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Volumn 111, Issue 4, 2014, Pages 583-589

Natural inhibitors of thrombin

Author keywords

Exosite; Inhibition; Protease; Regulation; Structure

Indexed keywords

ANOPHELIN; ANTITHROMBIN; HAEMADIN; HEPARIN COFACTOR II; HIRUDIN; ORNITHODORIN; PLASMINOGEN ACTIVATOR INHIBITOR 3; PROTEASE NEXIN I; RHODNIIN; SERINE PROTEASE THROMBIN; SERINE PROTEINASE INHIBITOR; THROMBIN; THROMBIN INHIBITOR; TRIABIN; UNCLASSIFIED DRUG; VARIEGIN; INSECT PROTEIN;

EID: 84897537641     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH13-10-0811     Document Type: Article
Times cited : (49)

References (56)
  • 2
    • 82755191913 scopus 로고    scopus 로고
    • Structural Insights into the Life History of Thrombin
    • In: Springer Japan
    • Huntington J. Structural Insights into the Life History of Thrombin. In: Recent Advances in Thrombosis and Hemostasis 2008: Springer Japan, 2008, pp. 80-106.
    • (2008) Recent Advances in Thrombosis and Hemostasis 2008 , pp. 80-106
    • Huntington, J.1
  • 3
    • 37049044629 scopus 로고
    • An Enzyme Cascade in the Blood Clotting Mechanism, and Its Function as a Biochemical Amplifier
    • Macfarlane RG. An Enzyme Cascade in the Blood Clotting Mechanism, and Its Function as a Biochemical Amplifier. Nature 1964; 202: 498-499.
    • (1964) Nature , vol.202 , pp. 498-499
    • McFarlane, R.G.1
  • 4
    • 37049242417 scopus 로고
    • Waterfall Sequence for Intrinsic Blood Clotting
    • Davie EW, Ratnoff OD. Waterfall Sequence for Intrinsic Blood Clotting. Science 1964; 145: 1310-1312.
    • (1964) Science , vol.145 , pp. 1310-1312
    • Davie, E.W.1    Ratnoff, O.D.2
  • 5
    • 33644874510 scopus 로고    scopus 로고
    • Rethinking the coagulation cascade
    • Hoffman MM, Monroe DM. Rethinking the coagulation cascade. Curr Hematol Rep 2005; 4: 391-396.
    • (2005) Curr Hematol Rep , vol.4 , pp. 391-396
    • Hoffman, M.M.1    Monroe, D.M.2
  • 6
    • 0034971291 scopus 로고    scopus 로고
    • A cell-based model of hemostasis
    • Hoffman M, Monroe DM, 3rd. A cell-based model of hemostasis. Thromb Haemost 2001; 85: 958-965.
    • (2001) Thromb Haemost , vol.85 , pp. 958-965
    • Hoffman, M.1    Monroe III, D.M.2
  • 7
    • 84857788797 scopus 로고    scopus 로고
    • Platelets and primary haemostasis
    • Clemetson KJ. Platelets and primary haemostasis. Thromb Res 2012; 129: 220-224.
    • (2012) Thromb Res , vol.129 , pp. 220-224
    • Clemetson, K.J.1
  • 8
    • 0022975591 scopus 로고
    • The prothrombinase-catalyzed activation of prothrombin proceeds through the intermediate meizothrombin in an ordered, sequential reaction
    • Krishnaswamy S, Mann KG, Nesheim ME. The prothrombinase-catalyzed activation of prothrombin proceeds through the intermediate meizothrombin in an ordered, sequential reaction. J Biol Chem 1986; 261: 8977-8984.
    • (1986) J Biol Chem , vol.261 , pp. 8977-8984
    • Krishnaswamy, S.1    Mann, K.G.2    Nesheim, M.E.3
  • 9
    • 33646470969 scopus 로고    scopus 로고
    • An overview of the structure and function of thrombin
    • Davie EW, Kulman JD. An overview of the structure and function of thrombin. Semin Thromb Hemost 2006; 32 (Suppl 1): 3-15.
    • (2006) Semin Thromb Hemost , vol.32 , Issue.SUPPL. 1 , pp. 3-15
    • Davie, E.W.1    Kulman, J.D.2
  • 10
    • 0027050807 scopus 로고
    • The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
    • Bode W, Turk D, Karshikov A. The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci 1992; 1: 426-471.
    • (1992) Protein Sci , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 11
    • 0034732094 scopus 로고    scopus 로고
    • Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex
    • Fuentes-Prior P, Iwanaga Y, Huber R, et al. Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex. Nature 2000; 404: 518-525.
    • (2000) Nature , vol.404 , pp. 518-525
    • Fuentes-Prior, P.1    Iwanaga, Y.2    Huber, R.3
  • 12
    • 1542297770 scopus 로고    scopus 로고
    • Crystal structure of the complex between thrombin and the central "E" region of fibrin
    • Pechik I, Madrazo J, Mosesson MW, et al. Crystal structure of the complex between thrombin and the central "E" region of fibrin. Proc Natl Acad Sci USA 2004; 101: 2718-2723.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2718-2723
    • Pechik, I.1    Madrazo, J.2    Mosesson, M.W.3
  • 13
    • 77952030606 scopus 로고    scopus 로고
    • Crystal structure of thrombin bound to the uncleaved extracellular fragment of PAR1
    • Gandhi PS, Chen Z, Di Cera E. Crystal structure of thrombin bound to the uncleaved extracellular fragment of PAR1. J Biol Chem 2010; 285: 15393-15398.
    • (2010) J Biol Chem , vol.285 , pp. 15393-15398
    • Gandhi, P.S.1    Chen, Z.2    Di Cera, E.3
  • 14
    • 0035816595 scopus 로고    scopus 로고
    • An extensive interaction interface between thrombin and factor V is required for factor V activation
    • Myles T, Yun TH, Hall SW, et al. An extensive interaction interface between thrombin and factor V is required for factor V activation. J Biol Chem 2001; 276: 25143-25149.
    • (2001) J Biol Chem , vol.276 , pp. 25143-25149
    • Myles, T.1    Yun, T.H.2    Hall, S.W.3
  • 15
    • 0037108447 scopus 로고    scopus 로고
    • Structural requirements for the activation of human factor VIII by thrombin
    • Myles T, Yun TH, Leung LL. Structural requirements for the activation of human factor VIII by thrombin. Blood 2002; 100: 2820-2826.
    • (2002) Blood , vol.100 , pp. 2820-2826
    • Myles, T.1    Yun, T.H.2    Leung, L.L.3
  • 16
    • 33745834732 scopus 로고    scopus 로고
    • The structural integrity of anion binding exosite I of thrombin is required and sufficient for timely cleavage and activation of factor V and factor VIII
    • Bukys MA, Orban T, Kim PY, et al. The structural integrity of anion binding exosite I of thrombin is required and sufficient for timely cleavage and activation of factor V and factor VIII. J Biol Chem 2006; 281: 18569-18580.
    • (2006) J Biol Chem , vol.281 , pp. 18569-18580
    • Bukys, M.A.1    Orban, T.2    Kim, P.Y.3
  • 17
    • 0033520366 scopus 로고    scopus 로고
    • Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains
    • Hall SW, Nagashima M, Zhao L, et al. Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains. J Biol Chem 1999; 274: 25510-25516.
    • (1999) J Biol Chem , vol.274 , pp. 25510-25516
    • Hall, S.W.1    Nagashima, M.2    Zhao, L.3
  • 18
    • 0021080275 scopus 로고
    • Promotion of thrombin-catalyzed activation of factor XIII by fibrinogen
    • Janus TJ, Lewis SD, Lorand L, et al. Promotion of thrombin-catalyzed activation of factor XIII by fibrinogen. Biochemistry 1983; 22: 6269-6272.
    • (1983) Biochemistry , vol.22 , pp. 6269-6272
    • Janus, T.J.1    Lewis, S.D.2    Lorand, L.3
  • 19
    • 0035818425 scopus 로고    scopus 로고
    • Structural and functional mapping of the thrombin domain involved in the binding to the platelet glycoprotein Ib
    • De Cristofaro R, De Candia E, Landolfi R, et al. Structural and functional mapping of the thrombin domain involved in the binding to the platelet glycoprotein Ib. Biochemistry 2001; 40: 13268-13273.
    • (2001) Biochemistry , vol.40 , pp. 13268-13273
    • De Cristofaro, R.1    De Candia, E.2    Landolfi, R.3
  • 20
    • 0037815126 scopus 로고    scopus 로고
    • Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha
    • Celikel R, McClintock RA, Roberts JR, et al. Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha. Science 2003; 301: 218-221.
    • (2003) Science , vol.301 , pp. 218-221
    • Celikel, R.1    McClintock, R.A.2    Roberts, J.R.3
  • 21
    • 0038157329 scopus 로고    scopus 로고
    • Crystal structure of the GpIbalpha-thrombin complex essential for platelet aggregation
    • Dumas JJ, Kumar R, Seehra J, et al. Crystal structure of the GpIbalpha-thrombin complex essential for platelet aggregation. Science 2003; 301: 222-226.
    • (2003) Science , vol.301 , pp. 222-226
    • Dumas, J.J.1    Kumar, R.2    Seehra, J.3
  • 22
    • 22844450455 scopus 로고    scopus 로고
    • Exosite-interactive regions in the A1 and A2 domains of factor VIII facilitate thrombin-catalyzed cleavage of heavy chain
    • Nogami K, Zhou Q, Myles T, et al. Exosite-interactive regions in the A1 and A2 domains of factor VIII facilitate thrombin-catalyzed cleavage of heavy chain. J Biol Chem 2005; 280: 18476-18487.
    • (2005) J Biol Chem , vol.280 , pp. 18476-18487
    • Nogami, K.1    Zhou, Q.2    Myles, T.3
  • 23
    • 36349026035 scopus 로고    scopus 로고
    • The role of thrombin exosites I and II in the activation of human coagulation factor V
    • Segers K, Dahlback B, Bock PE, et al. The role of thrombin exosites I and II in the activation of human coagulation factor V. J Biol Chem 2007; 282: 33915-33924.
    • (2007) J Biol Chem , vol.282 , pp. 33915-33924
    • Segers, K.1    Dahlback, B.2    Bock, P.E.3
  • 24
    • 70449397927 scopus 로고    scopus 로고
    • Molecular diversity of anticoagulants from haematophagous animals
    • Koh CY, Kini RM. Molecular diversity of anticoagulants from haematophagous animals. Thromb Haemost 2009; 102: 437-453.
    • (2009) Thromb Haemost , vol.102 , pp. 437-453
    • Koh, C.Y.1    Kini, R.M.2
  • 25
    • 77957900996 scopus 로고    scopus 로고
    • Platelet aggregation inhibitors from hematophagous animals
    • Francischetti IM. Platelet aggregation inhibitors from hematophagous animals. Toxicon 2010; 56: 1130-1144.
    • (2010) Toxicon , vol.56 , pp. 1130-1144
    • Francischetti, I.M.1
  • 26
    • 0029999679 scopus 로고    scopus 로고
    • Thrombin inhibitors of bloodsucking animals
    • Dodt J, Otte M, Strube KH, et al. Thrombin inhibitors of bloodsucking animals. Semin Thromb Hemost 1996; 22: 203-208.
    • (1996) Semin Thromb Hemost , vol.22 , pp. 203-208
    • Dodt, J.1    Otte, M.2    Strube, K.H.3
  • 27
    • 0034615564 scopus 로고    scopus 로고
    • Structural basis of the endoproteinase-protein inhibitor interaction
    • Bode W, Huber R. Structural basis of the endoproteinase-protein inhibitor interaction. Biochim Biophys Acta 2000; 1477: 241-252.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 241-252
    • Bode, W.1    Huber, R.2
  • 28
    • 77952738973 scopus 로고    scopus 로고
    • Leech-derived thrombin inhibitors: From structures to mechanisms to clinical applications
    • Corral-Rodriguez MA, Macedo-Ribeiro S, Pereira PJ, et al. Leech-derived thrombin inhibitors: from structures to mechanisms to clinical applications. J Med Chem 2010; 53: 3847-3861.
    • (2010) J Med Chem , vol.53 , pp. 3847-3861
    • Corral-Rodriguez, M.A.1    McEdo-Ribeiro, S.2    Pereira, P.J.3
  • 29
    • 0025329390 scopus 로고
    • The structure of a complex of recombinant hirudin and human alpha-thrombin
    • Rydel TJ, Ravichandran KG, Tulinsky A, et al. The structure of a complex of recombinant hirudin and human alpha-thrombin. Science 1990; 249: 277-280.
    • (1990) Science , vol.249 , pp. 277-280
    • Rydel, T.J.1    Ravichandran, K.G.2    Tulinsky, A.3
  • 30
    • 0025866812 scopus 로고
    • Refined structure of the hirudin-thrombin complex
    • Rydel TJ, Tulinsky A, Bode W, et al. Refined structure of the hirudin-thrombin complex. J Mol Biol 1991; 221: 583-601.
    • (1991) J Mol Biol , vol.221 , pp. 583-601
    • Rydel, T.J.1    Tulinsky, A.2    Bode, W.3
  • 31
    • 0025309452 scopus 로고
    • Crystal structure of the thrombin-hirudin complex: A novel mode of serine protease inhibition
    • Grutter MG, Priestle JP, Rahuel J, et al. Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition. EMBO J 1990; 9: 2361-2365.
    • (1990) EMBO J , vol.9 , pp. 2361-2365
    • Grutter, M.G.1    Priestle, J.P.2    Rahuel, J.3
  • 32
    • 0028784163 scopus 로고
    • Two heads are better than one: Crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin
    • van de Locht A, Lamba D, Bauer M, et al. Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin. EMBO J 1995; 14: 5149-5157.
    • (1995) EMBO J , vol.14 , pp. 5149-5157
    • van de Locht, A.1    Lamba, D.2    Bauer, M.3
  • 33
    • 0029957955 scopus 로고    scopus 로고
    • The ornithodorin-thrombin crystal structure, a key to the TAP enigma?
    • van de Locht A, Stubbs MT, Bode W, et al. The ornithodorin-thrombin crystal structure, a key to the TAP enigma? EMBO J 1996; 15: 6011-6017.
    • (1996) EMBO J , vol.15 , pp. 6011-6017
    • van de Locht, A.1    Stubbs, M.T.2    Bode, W.3
  • 34
    • 0015901579 scopus 로고
    • Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region
    • Ruhlmann A, Kukla D, Schwager P, et al. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region. J Mol Biol 1973; 77: 417-436.
    • (1973) J Mol Biol , vol.77 , pp. 417-436
    • Ruhlmann, A.1    Kukla, D.2    Schwager, P.3
  • 35
    • 0030666566 scopus 로고    scopus 로고
    • Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug
    • Fuentes-Prior P, Noeske-Jungblut C, Donner P, et al. Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug. Proc Natl Acad Sci USA 1997; 94: 11845-11850.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11845-11850
    • Fuentes-Prior, P.1    Noeske-Jungblut, C.2    Donner, P.3
  • 36
    • 0028792216 scopus 로고
    • Triabin, a highly potent exosite inhibitor of thrombin
    • Noeske-Jungblut C, Haendler B, Donner P, et al. Triabin, a highly potent exosite inhibitor of thrombin. J Biol Chem 1995; 270: 28629-28634.
    • (1995) J Biol Chem , vol.270 , pp. 28629-28634
    • Noeske-Jungblut, C.1    Haendler, B.2    Donner, P.3
  • 37
    • 0034329465 scopus 로고    scopus 로고
    • Crystal structure of the human alpha-thrombin-haemadin complex: An exosite II-binding inhibitor
    • Richardson JL, Kroger B, Hoeffken W, et al. Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor. EMBO J 2000; 19: 5650-5660.
    • (2000) EMBO J , vol.19 , pp. 5650-5660
    • Richardson, J.L.1    Kroger, B.2    Hoeffken, W.3
  • 38
    • 0031574020 scopus 로고    scopus 로고
    • New insights into the regulation of the blood clotting cascade derived from the X-ray crystal structure of bovine meizothrombin des F1 in complex with PPACK
    • Martin PD, Malkowski MG, Box J, et al. New insights into the regulation of the blood clotting cascade derived from the X-ray crystal structure of bovine meizothrombin des F1 in complex with PPACK. Structure 1997; 5: 1681-1693.
    • (1997) Structure , vol.5 , pp. 1681-1693
    • Martin, P.D.1    Malkowski, M.G.2    Box, J.3
  • 39
    • 0037176829 scopus 로고    scopus 로고
    • Characterization of the residues involved in the human alpha-thrombin-haemadin complex: An exosite II-binding inhibitor
    • Richardson JL, Fuentes-Prior P, Sadler JE, et al. Characterization of the residues involved in the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor. Biochemistry 2002; 41: 2535-2542.
    • (2002) Biochemistry , vol.41 , pp. 2535-2542
    • Richardson, J.L.1    Fuentes-Prior, P.2    Sadler, J.E.3
  • 40
    • 35748980268 scopus 로고    scopus 로고
    • Variegin, a novel fast and tight binding thrombin inhibitor from the tropical bont tick
    • Koh CY, Kazimirova M, Trimnell A, et al. Variegin, a novel fast and tight binding thrombin inhibitor from the tropical bont tick. J Biol Chem 2007; 282: 29101-29113.
    • (2007) J Biol Chem , vol.282 , pp. 29101-29113
    • Koh, C.Y.1    Kazimirova, M.2    Trimnell, A.3
  • 41
    • 80055037344 scopus 로고    scopus 로고
    • Crystal structure of thrombin in complex with S-variegin: Insights of a novel mechanism of inhibition and design of tunable thrombin inhibitors
    • Koh CY, Kumar S, Kazimirova M, et al. Crystal structure of thrombin in complex with S-variegin: insights of a novel mechanism of inhibition and design of tunable thrombin inhibitors. PloS one 2011; 6: e26367.
    • (2011) PloS one , vol.6
    • Koh, C.Y.1    Kumar, S.2    Kazimirova, M.3
  • 42
    • 84871839379 scopus 로고    scopus 로고
    • Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector
    • Figueiredo AC, de Sanctis D, Gutierrez-Gallego R, et al. Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. Proc Natl Acad Sci USA 2012; 109: E3649-3658.
    • (2012) Proc Natl Acad Sci USA , vol.109
    • Figueiredo, A.C.1    de Sanctis, D.2    Gutierrez-Gallego, R.3
  • 43
    • 84880605751 scopus 로고    scopus 로고
    • Thrombin inhibition by the serpins
    • Huntington JA. Thrombin inhibition by the serpins. J Thromb Haemost 2013; 11 (Suppl 1): 254-264.
    • (2013) J Thromb Haemost , vol.11 , Issue.SUPPL. 1 , pp. 254-264
    • Huntington, J.A.1
  • 44
    • 34250787144 scopus 로고    scopus 로고
    • Serpins in thrombosis, hemostasis and fibrinolysis
    • Rau JC, Beaulieu LM, Huntington JA, et al. Serpins in thrombosis, hemostasis and fibrinolysis. J Thromb Haemost 2007; 5 (Suppl 1): 102-115.
    • (2007) J Thromb Haemost , vol.5 , Issue.SUPPL. 1 , pp. 102-115
    • Rau, J.C.1    Beaulieu, L.M.2    Huntington, J.A.3
  • 45
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins PG. Serpin structure, mechanism, and function. Chem Rev 2002; 102: 4751-4804.
    • (2002) Chem Rev , vol.102 , pp. 4751-4804
    • Gettins, P.G.1
  • 46
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington JA, Read RJ, Carrell RW. Structure of a serpin-protease complex shows inhibition by deformation. Nature 2000; 407: 923-926.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 47
    • 4344590703 scopus 로고    scopus 로고
    • Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin
    • Li W, Johnson DJ, Esmon CT, et al. Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin. Nat Struct Mol Biol 2004; 11: 857-862.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 857-862
    • Li, W.1    Johnson, D.J.2    Esmon, C.T.3
  • 48
    • 0037143655 scopus 로고    scopus 로고
    • Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism
    • Baglin TP, Carrell RW, Church FC, et al. Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism. Proc Natl Acad Sci USA 2002; 99: 11079-11084.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11079-11084
    • Baglin, T.P.1    Carrell, R.W.2    Church, F.C.3
  • 49
    • 42449150052 scopus 로고    scopus 로고
    • Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex
    • Li W, Adams TE, Nangalia J, et al. Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex. Proc Natl Acad Sci USA 2008; 105: 4661-4666.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 4661-4666
    • Li, W.1    Adams, T.E.2    Nangalia, J.3
  • 50
    • 84864040805 scopus 로고    scopus 로고
    • Crystal structures of protease nexin-1 in complex with heparin and thrombin suggest a 2-step recognition mechanism
    • Li W, Huntington JA. Crystal structures of protease nexin-1 in complex with heparin and thrombin suggest a 2-step recognition mechanism. Blood 2012; 120: 459-467.
    • (2012) Blood , vol.120 , pp. 459-467
    • Li, W.1    Huntington, J.A.2
  • 51
    • 0035920162 scopus 로고    scopus 로고
    • The serpin inhibitory mechanism is critically dependent on the length of the reactive center loop
    • Zhou A, Carrell RW, Huntington JA. The serpin inhibitory mechanism is critically dependent on the length of the reactive center loop. J Biol Chem 2001; 276: 27541-27547.
    • (2001) J Biol Chem , vol.276 , pp. 27541-27547
    • Zhou, A.1    Carrell, R.W.2    Huntington, J.A.3
  • 52
    • 0035976896 scopus 로고    scopus 로고
    • Conformational changes in thrombin when complexed by serpins
    • Fredenburgh JC, Stafford AR, Weitz JI. Conformational changes in thrombin when complexed by serpins. J Biol Chem 2001; 276: 44828-44834.
    • (2001) J Biol Chem , vol.276 , pp. 44828-44834
    • Fredenburgh, J.C.1    Stafford, A.R.2    Weitz, J.I.3
  • 53
    • 0030791531 scopus 로고    scopus 로고
    • Inactivation of thrombin by antithrombin is accompanied by inactivation of regulatory exosite I
    • Bock PE, Olson ST, Bjork I. Inactivation of thrombin by antithrombin is accompanied by inactivation of regulatory exosite I. J Biol Chem 1997; 272: 19837-19845.
    • (1997) J Biol Chem , vol.272 , pp. 19837-19845
    • Bock, P.E.1    Olson, S.T.2    Bjork, I.3
  • 54
    • 78649654335 scopus 로고    scopus 로고
    • Thrombin inhibition by serpins disrupts exosite II
    • Li W, Johnson DJ, Adams TE, et al. Thrombin inhibition by serpins disrupts exosite II. J Biol Chem 2010; 285: 38621-38629.
    • (2010) J Biol Chem , vol.285 , pp. 38621-38629
    • Li, W.1    Johnson, D.J.2    Adams, T.E.3
  • 55
    • 0033010830 scopus 로고    scopus 로고
    • The clearance of thrombin-antithrombin and related serpin-enzyme complexes from the circulation: Role of various hepatocyte receptors
    • Wells MJ, Sheffield WP, Blajchman MA. The clearance of thrombin-antithrombin and related serpin-enzyme complexes from the circulation: role of various hepatocyte receptors. Thromb Haemost 1999; 81: 325-337.
    • (1999) Thromb Haemost , vol.81 , pp. 325-337
    • Wells, M.J.1    Sheffield, W.P.2    Blajchman, M.A.3
  • 56
    • 13244270050 scopus 로고    scopus 로고
    • Crystal structure of thrombin bound to heparin
    • Carter WJ, Cama E, Huntington JA. Crystal structure of thrombin bound to heparin. J Biol Chem 2005; 280: 2745-2749.
    • (2005) J Biol Chem , vol.280 , pp. 2745-2749
    • Carter, W.J.1    Cama, E.2    Huntington, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.