메뉴 건너뛰기




Volumn 148, Issue 4, 2010, Pages 467-479

Mechanisms and specificity of factor XIa and trypsin inhibition by protease nexin 2 and basic pancreatic trypsin inhibitor

Author keywords

BPTI; FXIa; inhibition mechanism; protease nexin 2 Kunitz domain; trypsin

Indexed keywords

ARGININE; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 11A; BLOOD CLOTTING FACTOR 12A; BLOOD CLOTTING FACTOR 7A; BLOOD CLOTTING FACTOR 9A; KALLIKREIN; LYSINE; PLASMIN; PROTEASE NEXIN; PROTEASE NEXIN 2; THROMBIN; TRYPSIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 77958070559     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvq080     Document Type: Article
Times cited : (24)

References (64)
  • 1
    • 42249109450 scopus 로고    scopus 로고
    • Serine peptidases: Classification, structure and function
    • Page, M.J. and Di Cera, E. (2008) Serine peptidases: classification, structure and function. Cell. Mol. Life Sci. 65, 1220-1236
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1220-1236
    • Page, M.J.1    Di Cera, E.2
  • 2
    • 0002800925 scopus 로고    scopus 로고
    • Factor XI
    • (Colman, R.W., Hirsh, J., Marder, V.J., Clowes, A.W., and George, J.N., eds.),Lippincott Williams&Wilkins, Philadelphia
    • Walsh, P.N. (2001) Factor XI, in Hemostasis and Thrombosis: Basic Principles&Clinical Practice(Colman, R.W., Hirsh, J., Marder, V.J., Clowes, A.W., and George, J.N., eds.), pp. 191-202, Lippincott Williams&Wilkins, Philadelphia
    • (2001) Hemostasis and Thrombosis: Basic Principles&Clinical Practice , pp. 191-202
    • Walsh, P.N.1
  • 3
    • 0017740353 scopus 로고
    • Human blood coagulation factor XI. Purification, properties, and mechanism of activation by activated factor XII
    • Bouma, B.N. and Griffin, J.H. (1977) Human blood coagulation factor XI. Purification, properties, and mechanism of activation by activated factor XII. J. Biol. Chem. 252, 6432-6437
    • (1977) J. Biol. Chem. , vol.252 , pp. 6432-6437
    • Bouma, B.N.1    Griffin, J.H.2
  • 4
    • 0025788582 scopus 로고
    • Activation of human blood coagulation factor XI independent of factor XII. Factor XI is activated by thrombin and factor XIa in the presence of negatively charged surfaces
    • Naito, K. and Fujikawa, K. (1991) Activation of human blood coagulation factor XI independent of factor XII. Factor XI is activated by thrombin and factor XIa in the presence of negatively charged surfaces. J. Biol. Chem. 266, 7353-7358
    • (1991) J. Biol. Chem. , vol.266 , pp. 7353-7358
    • Naito, K.1    Fujikawa, K.2
  • 5
    • 0025874052 scopus 로고
    • Factor XI activation in a revised model of blood coagulation
    • Gailani, D. and Broze, G.J. Jr (1991) Factor XI activation in a revised model of blood coagulation. Science 253, 909-912
    • (1991) Science , vol.253 , pp. 909-912
    • Gailani, D.1    Broze Jr., G.J.2
  • 6
    • 0019370191 scopus 로고
    • Contributions of human platelets to the proteolytic activation of blood coagulation factors XII and XI
    • Walsh, P.N. and Griffin, J.H. (1981) Contributions of human platelets to the proteolytic activation of blood coagulation factors XII and XI. Blood 57, 106-118
    • (1981) Blood , vol.57 , pp. 106-118
    • Walsh, P.N.1    Griffin, J.H.2
  • 7
    • 0016176380 scopus 로고
    • The mechanism of activation of bovine factor IX (Christmas factor) by bovine factor XIa (activated plasma thromboplastin antecedent)
    • Fujikawa, K., Legaz, M.E., Kato, H., and Davie, E.W. (1974) The mechanism of activation of bovine factor IX (Christmas factor) by bovine factor XIa (activated plasma thromboplastin antecedent). Biochemistry 13, 4508-4516
    • (1974) Biochemistry , vol.13 , pp. 4508-4516
    • Fujikawa, K.1    Legaz, M.E.2    Kato, H.3    Davie, E.W.4
  • 8
    • 0017900590 scopus 로고
    • Activation of human factor IX (Christmas factor
    • Di Scipio, R.G., Kurachi, K., and Davie, E.W. (1978) Activation of human factor IX (Christmas factor). J. Clin. Invest. 61, 1528-1538
    • (1978) J. Clin. Invest. , vol.61 , pp. 1528-1538
    • Di Scipio, R.G.1    Kurachi, K.2    Davie, E.W.3
  • 9
    • 0018118335 scopus 로고
    • Human blood coagulation factor IX. Purification, properties, and mechanism of activation by activated factor XI
    • Osterud, B., Bouma, B.N., and Griffin, J.H. (1978) Human blood coagulation factor IX. Purification, properties, and mechanism of activation by activated factor XI. J. Biol. Chem. 253, 5946-5951
    • (1978) J. Biol. Chem. , vol.253 , pp. 5946-5951
    • Osterud, B.1    Bouma, B.N.2    Griffin, J.H.3
  • 10
    • 0023198922 scopus 로고
    • Role of calciumions and the heavy chain of factor XIa in the activation of human coagulation factor IX
    • Sinha, D., Seaman, F.S., and Walsh, P.N. (1987) Role of calciumions and the heavy chain of factor XIa in the activation of human coagulation factor IX. Biochemistry 26, 3768-3775
    • (1987) Biochemistry , vol.26 , pp. 3768-3775
    • Sinha, D.1    Seaman, F.S.2    Walsh, P.N.3
  • 11
    • 0034528960 scopus 로고    scopus 로고
    • SERPIN regulation of factor XIa. The novel observation that protease nexin 1 in the presence of heparin is a more potent inhibitor of factor XIa than C1 inhibitor
    • Knauer, D.J., Majumdar, D., Fong, P.C., and Knauer, M.F. (2000) SERPIN regulation of factor XIa. The novel observation that protease nexin 1 in the presence of heparin is a more potent inhibitor of factor XIa than C1 inhibitor. J. Biol. Chem. 275, 37340-37346
    • (2000) J. Biol. Chem. , vol.275 , pp. 37340-37346
    • Knauer, D.J.1    Majumdar, D.2    Fong, P.C.3    Knauer, M.F.4
  • 12
    • 0015853889 scopus 로고
    • Anticoagulant action of heparin
    • Damus, P.S., Hicks, M., and Rosenberg, R.D. (1973) Anticoagulant action of heparin. Nature 246, 355-357
    • (1973) Nature , vol.246 , pp. 355-357
    • Damus, P.S.1    Hicks, M.2    Rosenberg, R.D.3
  • 13
    • 15844367087 scopus 로고    scopus 로고
    • Modulation of contact system proteases by glycosaminoglycans. Selective enhancement of the inhibition of factor XIa
    • Wuillemin, W.A., Eldering, E., Citarella, F., de Ruig, C.P., ten Cate, H., and Hack, C.E. (1996) Modulation of contact system proteases by glycosaminoglycans. Selective enhancement of the inhibition of factor XIa. J. Biol. Chem. 271, 12913-12918
    • (1996) J. Biol. Chem. , vol.271 , pp. 12913-12918
    • Wuillemin, W.A.1    Eldering, E.2    Citarella, F.3    De Ruig, C.P.4    Ten Cate, H.5    Hack, C.E.6
  • 14
    • 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. (1970) Inhibition of activated Hageman factor and activated plasma thromboplastin antecedent by purified serum C1 inactivator. J. Lab. Clin. Med. 76, 809-815
    • (1970) J. Lab. Clin. Med. , vol.76 , pp. 809-815
    • Forbes, C.D.1    Pensky, J.2    Ratnoff, O.D.3
  • 15
    • 0020048196 scopus 로고
    • Inactivation of factor XIa by plasma protease inhibitors: Predominant role of alpha 1-protease inhibitor and protective effect of high molecular weight kininogen
    • Scott, C.F., Schapira, M., James, H.L., Cohen, A.B., and Colman, R.W. (1982) Inactivation of factor XIa by plasma protease inhibitors: predominant role of alpha 1-protease inhibitor and protective effect of high molecular weight kininogen. J. Clin. Invest. 69, 844-852
    • (1982) J. Clin. Invest. , vol.69 , pp. 844-852
    • Scott, C.F.1    Schapira, M.2    James, H.L.3    Cohen, A.B.4    Colman, R.W.5
  • 16
    • 0016346287 scopus 로고
    • Substrates of Hageman factor.I. Isolation and characterization of human factor XI (PTA) and inhibition of the activated enzyme by alpha 1-antitrypsin
    • Heck, L.W. and Kaplan, A.P. (1974) Substrates of Hageman factor. I. Isolation and characterization of human factor XI (PTA) and inhibition of the activated enzyme by alpha 1-antitrypsin. J. Exp. Med. 140, 1615-1630
    • (1974) J. Exp. Med. , vol.140 , pp. 1615-1630
    • Heck, L.W.1    Kaplan, A.P.2
  • 18
    • 0025365401 scopus 로고
    • Platelet coagulation factor XIa-inhibitor, a form of Alzheimer amyloid precursor protein
    • Smith, R.P., Higuchi, D.A., and Broze, G.J. Jr (1990) Platelet coagulation factor XIa-inhibitor, a form of Alzheimer amyloid precursor protein. Science 248, 1126-1128
    • (1990) Science , vol.248 , pp. 1126-1128
    • Smith, R.P.1    Higuchi, D.A.2    Broze Jr., G.J.3
  • 19
    • 0025371509 scopus 로고
    • Protease nexin-II (amyloid beta-protein precursor): A platelet alpha-granule protein
    • Van Nostrand, W.E., Schmaier, A.H., Farrow, J.S., and Cunningham, D.D. (1990) Protease nexin-II (amyloid beta-protein precursor): a platelet alpha-granule protein. Science 248, 745-748
    • (1990) Science , vol.248 , pp. 745-748
    • Van Nostrand, W.E.1    Schmaier, A.H.2    Farrow, J.S.3    Cunningham, D.D.4
  • 21
    • 0025357613 scopus 로고
    • Immunopurification and protease inhibitory properties of protease nexin- 2/amyloid beta-protein precursor
    • Van Nostrand, W.E., Wagner, S.L., Farrow, J.S., and Cunningham, D.D. (1990) Immunopurification and protease inhibitory properties of protease nexin- 2/amyloid beta-protein precursor. J. Biol. Chem. 265, 9591-9594
    • (1990) J. Biol. Chem. , vol.265 , pp. 9591-9594
    • Van Nostrand, W.E.1    Wagner, S.L.2    Farrow, J.S.3    Cunningham, D.D.4
  • 22
    • 0030671397 scopus 로고    scopus 로고
    • The mechanism by which heparin promotes the inhibition of coagulation factor XIa by protease nexin-2
    • DOI 10.1074/jbc.272.42.26139
    • Zhang, Y., Scandura, J.M., Van Nostrand, W.E., and Walsh, P.N. (1997) The mechanism by which heparin promotes the inhibition of coagulation factor XIa by protease nexin-2. J. Biol. Chem. 272, 26139-26144 (Pubitemid 27458821)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.42 , pp. 26139-26144
    • Zhang, Y.1    Scandura, J.M.2    Van Nostrand, W.E.3    Walsh, P.N.4
  • 23
    • 0031020877 scopus 로고    scopus 로고
    • Progress curve analysis of the kinetics with which blood coagulation factor XIa is inhibited by protease nexin-2
    • Scandura, J.M., Zhang, Y., Van Nostrand, W.E., and Walsh, P.N. (1997) Progress curve analysis of the kinetics with which blood coagulation factor XIa is inhibited by protease nexin-2. Biochemistry 36, 412-420
    • (1997) Biochemistry , vol.36 , pp. 412-420
    • Scandura, J.M.1    Zhang, Y.2    Van Nostrand, W.E.3    Walsh, P.N.4
  • 24
    • 0034712682 scopus 로고    scopus 로고
    • Protease nexin II interactions with coagulation factor XIa are contained within the Kunitz protease inhibitor domain of protease nexin II and the factor XIa catalytic domain
    • Badellino, K.O. and Walsh, P.N. (2000) Protease nexin II interactions with coagulation factor XIa are contained within the Kunitz protease inhibitor domain of protease nexin II and the factor XIa catalytic domain. Biochemistry 39, 4769-4777
    • (2000) Biochemistry , vol.39 , pp. 4769-4777
    • Badellino, K.O.1    Walsh, P.N.2
  • 25
    • 0035954370 scopus 로고    scopus 로고
    • Localization of a heparin binding site in the catalytic domain of factor XIa
    • Badellino, K.O. and Walsh, P.N. (2001) Localization of a heparin binding site in the catalytic domain of factor XIa. Biochemistry 40, 7569-7580
    • (2001) Biochemistry , vol.40 , pp. 7569-7580
    • Badellino, K.O.1    Walsh, P.N.2
  • 26
    • 0034721778 scopus 로고    scopus 로고
    • Inhibition of six serine proteinases of the human coagulation system by mutants of bovine pancreatic trypsin inhibitor
    • Grzesiak, A., Krokoszynska, I., Krowarsch, D., Buczek, O., Dadlez, M., and Otlewski, J. (2000) Inhibition of six serine proteinases of the human coagulation system by mutants of bovine pancreatic trypsin inhibitor. J. Biol. Chem. 275, 33346-33352
    • (2000) J. Biol. Chem. , vol.275 , pp. 33346-33352
    • Grzesiak, A.1    Krokoszynska, I.2    Krowarsch, D.3    Buczek, O.4    Dadlez, M.5    Otlewski, J.6
  • 27
    • 0029087665 scopus 로고
    • Characterisation of a novel series of aprotinin-derived anticoagulants. I.In vitro and pharmacological properties
    • Stassen, J.M., Lambeir, A.M., Matthyssens, G., Ripka, W.C., Nystrom, A., Sixma, J.J., and Vermylen, J. (1995) Characterisation of a novel series of aprotinin-derived anticoagulants. I. In vitro and pharmacological properties. Thromb. Haemost. 74, 646-654
    • (1995) Thromb. Haemost. , vol.74 , pp. 646-654
    • Stassen, J.M.1    Lambeir, A.M.2    Matthyssens, G.3    Ripka, W.C.4    Nystrom, A.5    Sixma, J.J.6    Vermylen, J.7
  • 28
    • 27744571272 scopus 로고    scopus 로고
    • Structural and mutational analyses of the molecular interactions between the catalytic domain of factor XIa and the Kunitz protease inhibitor domain of protease nexin 2
    • Navaneetham, D., Jin, L., Pandey, P., Strickler, J.E., Babine, R.E., Abdel-Meguid, S.S., and Walsh, P.N. (2005) Structural and mutational analyses of the molecular interactions between the catalytic domain of factor XIa and the Kunitz protease inhibitor domain of protease nexin 2. J. Biol. Chem. 280, 36165-36175
    • (2005) J. Biol. Chem. , vol.280 , pp. 36165-36175
    • Navaneetham, D.1    Jin, L.2    Pandey, P.3    Strickler, J.E.4    Babine, R.E.5    Abdel-Meguid, S.S.6    Walsh, P.N.7
  • 29
    • 33846322485 scopus 로고    scopus 로고
    • Rigidification of a flexible protease inhibitor variant upon binding to trypsin
    • Hanson, W.M., Domek, G.J., Horvath, M.P., and Goldenberg, D.P. (2007) Rigidification of a flexible protease inhibitor variant upon binding to trypsin. J. Mol. Biol. 366, 230-243
    • (2007) J. Mol. Biol. , vol.366 , pp. 230-243
    • Hanson, W.M.1    Domek, G.J.2    Horvath, M.P.3    Goldenberg, D.P.4
  • 30
    • 34748920109 scopus 로고    scopus 로고
    • Aprotinin in cardiac surgery: A review of conventional and novel mechanisms of action
    • McEvoy, M.D., Reeves, S.T., Reves, J.G., and Spinale, F.G. (2007) Aprotinin in cardiac surgery: a review of conventional and novel mechanisms of action. Anesth. Analg. 105, 949-962
    • (2007) Anesth. Analg. , vol.105 , pp. 949-962
    • McEvoy, M.D.1    Reeves, S.T.2    Reves, J.G.3    Spinale, F.G.4
  • 31
    • 58849137661 scopus 로고    scopus 로고
    • The safety of aprotinin and lysine-derived antifibrinolytic drugs in cardiac surgery: A meta-analysis
    • Henry, D., Carless, P., Fergusson, D., and Laupacis, A. (2009) The safety of aprotinin and lysine-derived antifibrinolytic drugs in cardiac surgery: a meta-analysis. CMAJ 180, 183-193
    • (2009) CMAJ , vol.180 , pp. 183-193
    • Henry, D.1    Carless, P.2    Fergusson, D.3    Laupacis, A.4
  • 32
    • 0023277889 scopus 로고
    • Kinetics of inhibition of human plasma kallikrein by a site-specific modified inhibitor Arg15-aprotinin: Evaluation using a microplate system and comparison with other proteases
    • Scott, C.F., Wenzel, H.R., Tschesche, H.R., and Colman, R.W. (1987) Kinetics of inhibition of human plasma kallikrein by a site-specific modified inhibitor Arg15-aprotinin: evaluation using a microplate system and comparison with other proteases. Blood 69, 1431-1436
    • (1987) Blood , vol.69 , pp. 1431-1436
    • Scott, C.F.1    Wenzel, H.R.2    Tschesche, H.R.3    Colman, R.W.4
  • 33
    • 42949108853 scopus 로고    scopus 로고
    • Structural basis for accelerated cleavage of bovine pancreatic trypsin inhibitor (BPTI) by human mesotrypsin
    • Salameh, M.A., Soares, A.S., Hockla, A., and Radisky, E.S. (2008) Structural basis for accelerated cleavage of bovine pancreatic trypsin inhibitor (BPTI) by human mesotrypsin. J. Biol. Chem. 283, 4115-4123.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4115-4123
    • Salameh, M.A.1    Soares, A.S.2    Hockla, A.3    Radisky, E.S.4
  • 34
    • 0025375504 scopus 로고    scopus 로고
    • Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa
    • Waxman, L., Smith, D.E., Arcuri, K.E., and Vlasuk, G.P. (1990) Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa. Science 248, 593-596.
    • (2008) Science , vol.248 , pp. 593-596
    • Waxman, L.1    Smith, D.E.2    Arcuri, K.E.3    Vlasuk, G.P.4
  • 35
    • 0028287885 scopus 로고
    • Assembly of the prothrombinase complex enhances the inhibition of bovine factor Xa by tick anticoagulant peptide
    • Krishnaswamy, S., Vlasuk, G.P., and Bergum, P.W. (1994) Assembly of the prothrombinase complex enhances the inhibition of bovine factor Xa by tick anticoagulant peptide. Biochemistry 33, 7897-7907
    • (1994) Biochemistry , vol.33 , pp. 7897-7907
    • Krishnaswamy, S.1    Vlasuk, G.P.2    Bergum, P.W.3
  • 36
    • 1642341747 scopus 로고    scopus 로고
    • Kinetics of factor Xa inhibition by recombinant tick anticoagulant peptide: Both active site and exosite interactions are required for a slow- and tight-binding inhibition mechanism
    • Rezaie, A.R. (2004) Kinetics of factor Xa inhibition by recombinant tick anticoagulant peptide: both active site and exosite interactions are required for a slow- and tight-binding inhibition mechanism. Biochemistry 43, 3368-3375
    • (2004) Biochemistry , vol.43 , pp. 3368-3375
    • Rezaie, A.R.1
  • 38
    • 0030033356 scopus 로고    scopus 로고
    • Inhibitory properties of separate recombinant Kunitz-type-protease- inhibitor domains from tissue-factor-pathway inhibitor
    • Petersen, L.C., Bjorn, S.E., Olsen, O.H., Nordfang, O., Norris, F., and Norris, K. (1996) Inhibitory properties of separate recombinant Kunitz-type-protease-inhibitor domains from tissue-factor-pathway inhibitor. Eur. J. Biochem. 235, 310-316
    • (1996) Eur. J. Biochem. , vol.235 , pp. 310-316
    • Petersen, L.C.1    Bjorn, S.E.2    Olsen, O.H.3    Nordfang, O.4    Norris, F.5    Norris, K.6
  • 39
    • 36349029749 scopus 로고    scopus 로고
    • The role of tissue factor pathway inhibitor-2 in cancer biology
    • Sierko, E., Wojtukiewicz, M.Z., and Kisiel, W. (2007) The role of tissue factor pathway inhibitor-2 in cancer biology. Semin. Thromb. Hemost. 33, 653-659
    • (2007) Semin. Thromb. Hemost. , vol.33 , pp. 653-659
    • Sierko, E.1    Wojtukiewicz, M.Z.2    Kisiel, W.3
  • 40
    • 0029123833 scopus 로고
    • Enhanced plasmin inhibition by a reactive center lysine mutant of the Kunitz-type protease inhibitor domain of the amyloid beta-protein precursor
    • Van Nostrand, W.E., Schmaier, A.H., Siegel, R.S., Wagner, S.L., and Raschke, W.C. (1995) Enhanced plasmin inhibition by a reactive center lysine mutant of the Kunitz-type protease inhibitor domain of the amyloid beta-protein precursor. J. Biol. Chem. 270, 22827-22830
    • (1995) J. Biol. Chem. , vol.270 , pp. 22827-22830
    • Van Nostrand, W.E.1    Schmaier, A.H.2    Siegel, R.S.3    Wagner, S.L.4    Raschke, W.C.5
  • 41
    • 0030794907 scopus 로고    scopus 로고
    • Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid beta-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): Engineering of inhibitors with altered specificities
    • Scheidig, A.J., Hynes, T.R., Pelletier, L.A., Wells, J.A., and Kossiakoff, A.A. (1997) Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid beta-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): engineering of inhibitors with altered specificities. Protein Sci. 6, 1806-1824
    • (1997) Protein Sci. , vol.6 , pp. 1806-1824
    • Scheidig, A.J.1    Hynes, T.R.2    Pelletier, L.A.3    Wells, J.A.4    Kossiakoff, A.A.5
  • 42
    • 0027300523 scopus 로고
    • Crystal structures of rat anionic trypsin complexed with the protein inhibitors APPI and BPTI
    • Perona, J.J., Tsu, C.A., Craik, C.S., and Fletterick, R.J. (1993) Crystal structures of rat anionic trypsin complexed with the protein inhibitors APPI and BPTI. J. Mol. Biol. 230, 919-933
    • (1993) J. Mol. Biol. , vol.230 , pp. 9190-933
    • Perona, J.J.1    Tsu, C.A.2    Craik, C.S.3    Fletterick, R.J.4
  • 43
    • 0025008384 scopus 로고
    • X-ray crystal structure of the protease inhibitor domain of Alzheimer's amyloid beta-protein precursor
    • Hynes, T.R., Randal, M., Kennedy, L.A., Eigenbrot, C., and Kossiakoff, A.A. (1990) X-ray crystal structure of the protease inhibitor domain of Alzheimer's amyloid beta-protein precursor. Biochemistry 29, 10018-10022
    • (1990) Biochemistry , vol.29 , pp. 10018-10022
    • Hynes, T.R.1    Randal, M.2    Kennedy, L.A.3    Eigenbrot, C.4    Kossiakoff, A.A.5
  • 44
    • 0024583557 scopus 로고
    • Kinetics of trypsin inhibition by its specific inhibitors
    • Zhou, J.M., Liu, C., and Tsou, C.L. (1989) Kinetics of trypsin inhibition by its specific inhibitors. Biochemistry 28, 1070-1076
    • (1989) Biochemistry , vol.28 , pp. 1070-1076
    • Zhou, J.M.1    Liu, C.2    Tsou, C.L.3
  • 45
    • 33747354633 scopus 로고    scopus 로고
    • Heparin modulates the 99-loop of factor IXa: Effects on reactivity with isolated Kunitz-type inhibitor domains
    • Neuenschwander, P.F., Williamson, S.R., Nalian, A., and Baker-Deadmond, K.J. (2006) Heparin modulates the 99-loop of factor IXa: effects on reactivity with isolated Kunitz-type inhibitor domains. J. Biol. Chem. 281, 23066-23074
    • (2006) J. Biol. Chem. , vol.281 , pp. 23066-23074
    • Neuenschwander, P.F.1    Williamson, S.R.2    Nalian, A.3    Baker-Deadmond, K.J.4
  • 46
    • 0016700753 scopus 로고
    • Tight-binding inhibitors-I. Kinetic behavior
    • Cha, S. (1975) Tight-binding inhibitors-I. Kinetic behavior. Biochem. Pharmacol. 24, 2177-2185
    • (1975) Biochem. Pharmacol. , vol.24 , pp. 2177-2185
    • Cha, S.1
  • 47
    • 0001396685 scopus 로고
    • The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions
    • Morrison, J.F. (1982) The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions. Trends Biochem. Sci. 7, 102-105
    • (1982) Trends Biochem. Sci. , vol.7 , pp. 102-105
    • Morrison, J.F.1
  • 48
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison, J.F. and Walsh, C.T. (1988) The behavior and significance of slow-binding enzyme inhibitors. Adv. Enzymol. Relat. Areas Mol. Biol. 61, 201-301
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 49
    • 0027724106 scopus 로고
    • Kinetics of factor Xa inhibition by tissue factor pathway inhibitor
    • Huang, Z.F., Wun, T.C., and Broze, G.J. Jr (1993) Kinetics of factor Xa inhibition by tissue factor pathway inhibitor. J. Biol. Chem. 268, 26950-26955
    • (1993) J. Biol. Chem. , vol.268 , pp. 26950-26955
    • Huang, Z.F.1    Wun, T.C.2    Broze Jr., G.J.3
  • 50
    • 0015387337 scopus 로고
    • Trypsinpancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges
    • Vincent, J.P. and Lazdunski, M. (1972) Trypsinpancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges. Biochemistry 11, 2967-2977
    • (1972) Biochemistry , vol.11 , pp. 2967-2977
    • Vincent, J.P.1    Lazdunski, M.2
  • 51
    • 0037064001 scopus 로고    scopus 로고
    • The interaction of factor XIa with activated platelets but not endothelial cells promotes the activation of factor IX in the consolidation phase of blood coagulation
    • Baird, T.R. and Walsh, P.N. (2002) The interaction of factor XIa with activated platelets but not endothelial cells promotes the activation of factor IX in the consolidation phase of blood coagulation. J. Biol. Chem. 277, 38462-38467
    • (2002) J. Biol. Chem. , vol.277 , pp. 38462-38467
    • Baird, T.R.1    Walsh, P.N.2
  • 55
    • 0028100458 scopus 로고
    • Kunitz domain inhibitors of tissue factor-factor VIIa.II. Potent and specific inhibitors by competitive phage selection
    • Dennis, M.S. and Lazarus, R.A. (1994) Kunitz domain inhibitors of tissue factor-factor VIIa. II. Potent and specific inhibitors by competitive phage selection. J. Biol. Chem. 269, 22137-22144
    • (1994) J. Biol. Chem. , vol.269 , pp. 22137-22144
    • Dennis, M.S.1    Lazarus, R.A.2
  • 57
    • 0028924689 scopus 로고
    • Factor IXa inhibition by protease nexin-2/amyloid beta-protein precursor on phospholipid vesicles and cell membranes
    • Schmaier, A.H., Dahl, L.D., Hasan, A.A., Cines, D.B., Bauer, K.A., and Van Nostrand, W.E. (1995) Factor IXa inhibition by protease nexin-2/amyloid beta-protein precursor on phospholipid vesicles and cell membranes. Biochemistry 34, 1171-1178
    • (1995) Biochemistry , vol.34 , pp. 1171-1178
    • Schmaier, A.H.1    Dahl, L.D.2    Hasan, A.A.3    Cines, D.B.4    Bauer, K.A.5    Van Nostrand, W.E.6
  • 58
    • 0028787671 scopus 로고
    • Protease nexin-2/amyloid beta-protein precursor inhibits factor Xa in the prothrombinase complex
    • Mahdi, F., Van Nostrand, W.E., and Schmaier, A.H. (1995) Protease nexin-2/amyloid beta-protein precursor inhibits factor Xa in the prothrombinase complex. J. Biol. Chem. 270, 23468-23474
    • (1995) J. Biol. Chem. , vol.270 , pp. 23468-23474
    • Mahdi, F.1    Van Nostrand, W.E.2    Schmaier, A.H.3
  • 59
    • 0034209755 scopus 로고    scopus 로고
    • Protease nexin-2/Amyloid beta-protein precursor regulates factor VIIa and the factor VIIa-tissue factor complex
    • Mahdi, F., Rehemtulla, A., Van Nostrand, W.E., Bajaj, S.P., and Schmaier, A.H. (2000) Protease nexin-2/ Amyloid beta-protein precursor regulates factor VIIa and the factor VIIa-tissue factor complex. Thromb. Res. 99, 267-276
    • (2000) Thromb. Res. , vol.99 , pp. 267-276
    • Mahdi, F.1    Rehemtulla, A.2    Van Nostrand, W.E.3    Bajaj, S.P.4    Schmaier, A.H.5
  • 60
    • 0029766569 scopus 로고    scopus 로고
    • Alanine point-mutations in the reactive region of bovine pancreatic trypsin inhibitor: Effects on the kinetics and thermodynamics of binding to beta-trypsin and alphachymotrypsin
    • Castro, M.J. and Anderson, S. (1996) Alanine point-mutations in the reactive region of bovine pancreatic trypsin inhibitor: effects on the kinetics and thermodynamics of binding to beta-trypsin and alphachymotrypsin. Biochemistry 35, 11435-11446
    • (1996) Biochemistry , vol.35 , pp. 11435-11446
    • Castro, M.J.1    Anderson, S.2
  • 61
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode, W. and Huber, R. (1992) Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204, 433-451
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 62
  • 63
    • 0033168389 scopus 로고    scopus 로고
    • The three-dimensional structure of Asp189Ser trypsin provides evidence for an inherent structural plasticity of the protease
    • Szabo, E., Bocskei, Z., Naray-Szabo, G., and Graf, L. (1999) The three-dimensional structure of Asp189Ser trypsin provides evidence for an inherent structural plasticity of the protease. Eur. J. Biochem. 263, 20-26
    • (1999) Eur. J. Biochem. , vol.263 , pp. 20-26
    • Szabo, E.1    Bocskei, Z.2    Naray-Szabo, G.3    Graf, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.