메뉴 건너뛰기




Volumn , Issue , 2011, Pages 239-254

Thrombin inhibitors from haematophagous animals

Author keywords

[No Author keywords available]

Indexed keywords


EID: 79960626665     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-90-481-9295-3_15     Document Type: Chapter
Times cited : (9)

References (62)
  • 1
    • 0021305732 scopus 로고
    • Interaction between blood-sucking arthropods and their hosts, and its influence on vector potential
    • Balashov, Y., 1984. Interaction between blood-sucking arthropods and their hosts, and its influence on vector potential. Annu. Rev. Entomol. 29, 137-156.
    • (1984) Annu. Rev. Entomol. , vol.29 , pp. 137-156
    • Balashov, Y.1
  • 2
    • 0025936157 scopus 로고
    • Role of interactions involving C-terminal nonpolar residues of hirudin in the formation of the thrombin-hirudin complex
    • Betz, A., Hofsteenge, J., Stone, S.R., 1991. Role of interactions involving C-terminal nonpolar residues of hirudin in the formation of the thrombin-hirudin complex. Biochemistry 30, 9848-9853.
    • (1991) Biochemistry , vol.30 , pp. 9848-9853
    • Betz, A.1    Hofsteenge, J.2    Stone, S.R.3
  • 3
    • 0026633347 scopus 로고
    • Interaction of the N-terminal region of hirudin with the active-site cleft of thrombin
    • Betz, A., Hofsteenge, J., Stone, S.R., 1992. Interaction of the N-terminal region of hirudin with the active-site cleft of thrombin. Biochemistry 31, 4557-4562.
    • (1992) Biochemistry , vol.31 , pp. 4557-4562
    • Betz, A.1    Hofsteenge, J.2    Stone, S.R.3
  • 4
    • 0027050807 scopus 로고
    • The refined 1.9-A X-ray crystal structure of D-Phe- Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
    • Bode, W., Turk, D., Karshikov, A., 1992. The refined 1.9-A X-ray crystal structure of D-Phe- Pro-Arg chloromethylketone-inhibited human α-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci. 1, 426-471.
    • (1992) Protein Sci , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 5
    • 0023766115 scopus 로고
    • Use of site-directed mutagenesis to investigate the basis for the specificity of hirudin
    • Braun, P.J., Dennis, S., Hofsteenge, J., Stone, S.R., 1988. Use of site-directed mutagenesis to investigate the basis for the specificity of hirudin. Biochemistry 27, 6517-6522.
    • (1988) Biochemistry , vol.27 , pp. 6517-6522
    • Braun, P.J.1    Dennis, S.2    Hofsteenge, J.3    Stone, S.R.4
  • 6
    • 0036712320 scopus 로고    scopus 로고
    • Infestin, a thrombin inhibitor presents in Triatoma infestans midgut, a Chagas' disease vector: Gene cloning, expression and characterization of the inhibitor
    • Campos, I.T., Amino, R., Sampaio, C.A., Auerswald, E.A., Friedrich, T., Lemaire, H.G., Schenkman, S., Tanaka, A.S., 2002. Infestin, a thrombin inhibitor presents in Triatoma infestans midgut, a Chagas' disease vector: gene cloning, expression and characterization of the inhibitor. Insect Biochem. Mol. Biol. 32, 991-997.
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 991-997
    • Campos, I.T.1    Amino, R.2    Sampaio, C.A.3    Auerswald, E.A.4    Friedrich, T.5    Lemaire, H.G.6    Schenkman, S.7    Tanaka, A.S.8
  • 8
    • 0013586606 scopus 로고
    • The conformations of hirudin in solution: A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics
    • Clore, G.M., Sukumaran, D.K., Nilges, M., Zarbock, J., Gronenborn, A.M., 1987. The conformations of hirudin in solution: A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J. 6, 529-537.
    • (1987) EMBO J , vol.6 , pp. 529-537
    • Clore, G.M.1    Sukumaran, D.K.2    Nilges, M.3    Zarbock, J.4    Gronenborn, A.M.5
  • 10
    • 0026337077 scopus 로고
    • The coagulation cascade: Initiation, maintenance, and regulation
    • Davie, E.W., Fujikawa, K., Kisiel, W., 1991. The coagulation cascade: initiation, maintenance, and regulation. Biochemistry 30, 10363-10370.
    • (1991) Biochemistry , vol.30 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 11
    • 0141484541 scopus 로고    scopus 로고
    • Thrombin interactions
    • Di Cera, E., 2003. Thrombin interactions. Chest 124, 11S-17S.
    • (2003) Chest , vol.124 , pp. 11S-17S
    • Di Cera, E.1
  • 12
    • 0023841705 scopus 로고
    • Interaction of site specific hirudin variants with α-thrombin
    • Dodt, J., Kohler, S., Baici, A., 1988. Interaction of site specific hirudin variants with α-thrombin. FEBS Lett. 229, 87-90.
    • (1988) FEBS Lett , vol.229 , pp. 87-90
    • Dodt, J.1    Kohler, S.2    Baici, A.3
  • 13
    • 0021331392 scopus 로고
    • The complete amino acid sequence of hirudin, a thrombin specific inhibitor: Application of colour carboxymethylation
    • Dodt, J., Muller, H.P., Seemuller, U., Chang, J.Y., 1984. The complete amino acid sequence of hirudin, a thrombin specific inhibitor: Application of colour carboxymethylation. FEBS Lett. 165, 180-184.
    • (1984) FEBS Lett , vol.165 , pp. 180-184
    • Dodt, J.1    Muller, H.P.2    Seemuller, U.3    Chang, J.Y.4
  • 14
    • 0020480240 scopus 로고
    • Thermodynamics and kinetics of single residue replacements in avian ovomucoid third domains: Effect on inhibitor interactions with serine proteinases
    • Empie, M.W., Laskowski, M. Jr., 1982. Thermodynamics and kinetics of single residue replacements in avian ovomucoid third domains: effect on inhibitor interactions with serine proteinases. Biochemistry 21, 2274-2284.
    • (1982) Biochemistry , vol.21 , pp. 2274-2284
    • Empie, M.W.1    Laskowski, M.2
  • 15
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: Structure and function
    • Flower, D.R., 1996. The lipocalin protein family: structure and function. Biochem. J. 318(Pt 1), 1-14.
    • (1996) Biochem. J , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 17
    • 43949108861 scopus 로고    scopus 로고
    • The direct thrombin inhibitor hirudin
    • Greinacher, A., Warkentin, T.E., 2008. The direct thrombin inhibitor hirudin. Thromb. Haemost. 99, 819-829.
    • (2008) Thromb. Haemost. , vol.99 , pp. 819-829
    • Greinacher, A.1    Warkentin, T.E.2
  • 18
    • 0028773897 scopus 로고
    • Proteinase inhibitors: Another new fold
    • Grutter, M.G., 1994. Proteinase inhibitors: Another new fold. Structure 2, 575-576.
    • (1994) Structure , vol.2 , pp. 575-576
    • Grutter, M.G.1
  • 20
    • 0024403533 scopus 로고
    • Conformation of recombinant desulfatohirudin in aqueous solution determined by nuclear magnetic resonance
    • Haruyama, H., Wuthrich, K., 1989. Conformation of recombinant desulfatohirudin in aqueous solution determined by nuclear magnetic resonance. Biochemistry 28, 4301-4312.
    • (1989) Biochemistry , vol.28 , pp. 4301-4312
    • Haruyama, H.1    Wuthrich, K.2
  • 21
    • 27144505651 scopus 로고    scopus 로고
    • Molecular recognition mechanisms of thrombin
    • Huntington, J.A., 2005. Molecular recognition mechanisms of thrombin. J. Thromb. Haemost. 3, 1861-1872.
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 1861-1872
    • Huntington, J.A.1
  • 22
    • 50849101992 scopus 로고    scopus 로고
    • How Na+ activates thrombin - A review of the functional and structural data
    • Huntington, J.A., 2008. How Na+ activates thrombin - A review of the functional and structural data. Biol. Chem. 389, 1025-1035.
    • (2008) Biol. Chem. , vol.389 , pp. 1025-1035
    • Huntington, J.A.1
  • 23
    • 0034008935 scopus 로고    scopus 로고
    • The insect salivary protein, prolixin-S, inhibits factor IXa generation and Xase complex formation in the blood coagulation pathway
    • Isawa, H., Yuda, M., Yoneda, K., Chinzei, Y., 2000. The insect salivary protein, prolixin-S, inhibits factor IXa generation and Xase complex formation in the blood coagulation pathway. J. Biol. Chem. 275, 6636-6641.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6636-6641
    • Isawa, H.1    Yuda, M.2    Yoneda, K.3    Chinzei, Y.4
  • 24
    • 0026720044 scopus 로고
    • Intrinsic fluorescence changes and rapid kinetics of the reaction of thrombin with hirudin
    • Jackman, M.P., Parry, M.A., Hofsteenge, J., Stone, S.R., 1992. Intrinsic fluorescence changes and rapid kinetics of the reaction of thrombin with hirudin. J. Biol. Chem. 267, 15375-15383.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15375-15383
    • Jackman, M.P.1    Parry, M.A.2    Hofsteenge, J.3    Stone, S.R.4
  • 26
  • 27
    • 70349401816 scopus 로고    scopus 로고
    • Anticoagulants from hematophagous animals
    • Koh, C.Y., Kini, R.M., 2008. Anticoagulants from hematophagous animals. Expert Rev. Hematol. 1, 135-139.
    • (2008) Expert Rev. Hematol. , vol.1 , pp. 135-139
    • Koh, C.Y.1    Kini, R.M.2
  • 28
    • 70449397927 scopus 로고    scopus 로고
    • Molecular diversity of anticoagulants from haematophagous animals
    • Koh, C.Y., Kini, R.M., 2009. Molecular diversity of anticoagulants from haematophagous animals. Thromb. Haemost. 102, 437-453.
    • (2009) Thromb. Haemost. , vol.102 , pp. 437-453
    • Koh, C.Y.1    Kini, R.M.2
  • 29
    • 7544249123 scopus 로고    scopus 로고
    • A thrombin inhibitor from the ixodid tick, Amblyomma hebraeum
    • Lai, R., Takeuchi, H., Jonczy, J., Rees, H.H., Turner, P.C., 2004. A thrombin inhibitor from the ixodid tick, Amblyomma hebraeum. Gene 342, 243-249.
    • (2004) Gene , vol.342 , pp. 243-249
    • Lai, R.1    Takeuchi, H.2    Jonczy, J.3    Rees, H.H.4    Turner, P.C.5
  • 31
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski, M. Jr., Kato, I., 1980. Protein inhibitors of proteinases. Annu. Rev. Biochem. 49, 593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 33
    • 34848863112 scopus 로고    scopus 로고
    • Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin
    • Liu, C.C., Brustad, E., Liu, W., Schultz, P.G., 2007. Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin. J. Am. Chem. Soc. 129, 10648-10649.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10648-10649
    • Liu, C.C.1    Brustad, E.2    Liu, W.3    Schultz, P.G.4
  • 35
    • 36749092203 scopus 로고    scopus 로고
    • Characterization of anti-hemostatic factors in the argasid, Argas monolakensis: Implications for the evolution of blood-feeding in the soft tick family
    • Mans, B.J., Andersen, J.F., Schwan, T.G., Ribeiro, J.M., 2008. Characterization of anti-hemostatic factors in the argasid, Argas monolakensis: implications for the evolution of blood-feeding in the soft tick family. Insect Biochem. Mol. Biol. 38, 22-41.
    • (2008) Insect Biochem. Mol. Biol. , vol.38 , pp. 22-41
    • Mans, B.J.1    Andersen, J.F.2    Schwan, T.G.3    Ribeiro, J.M.4
  • 36
    • 0036791106 scopus 로고    scopus 로고
    • Evolution of hematophagy in ticks: Common origins for blood coagulation and platelet aggregation inhibitors from soft ticks of the genus Ornithodoros
    • Mans, B.J., Louw, A.I., Neitz, A.W., 2002. Evolution of hematophagy in ticks: common origins for blood coagulation and platelet aggregation inhibitors from soft ticks of the genus Ornithodoros. Mol. Biol. Evol. 19, 1695-1705.
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 1695-1705
    • Mans, B.J.1    Louw, A.I.2    Neitz, A.W.3
  • 37
    • 0023127092 scopus 로고
    • Rapid purification and revised amino-terminal sequence of hirudin: A specific thrombin inhibitor of the bloodsucking leech
    • Mao, S.J., Yates, M.T., Blankenship, D.T., Cardin, A.D., Krstenansky, J.L., Lovenberg, W., Jackson, R.L., 1987. Rapid purification and revised amino-terminal sequence of hirudin: A specific thrombin inhibitor of the bloodsucking leech. Anal. Biochem. 161, 514-518.
    • (1987) Anal. Biochem. , vol.161 , pp. 514-518
    • Mao, S.J.1    Yates, M.T.2    Blankenship, D.T.3    Cardin, A.D.4    Krstenansky, J.L.5    Lovenberg, W.6    Jackson, R.L.7
  • 38
    • 0027968823 scopus 로고
    • The development of hirudin as an antithrombotic drug
    • Markwardt, F., 1994. The development of hirudin as an antithrombotic drug. Thromb. Res. 74, 1-23.
    • (1994) Thromb. Res. , vol.74 , pp. 1-23
    • Markwardt, F.1
  • 39
    • 0038474360 scopus 로고    scopus 로고
    • Dipetalogastin, a potent thrombin inhibitor from the blood-sucking insect, Dipetalogaster maximus cDNA cloning, expression and characterization
    • Mende, K., Petoukhova, O., Koulitchkova, V., Schaub, G.A., Lange, U., Kaufmann, R., Nowak, G., 1999. Dipetalogastin, a potent thrombin inhibitor from the blood-sucking insect. Dipetalogaster maximus cDNA cloning, expression and characterization. Eur. J. Biochem. 266, 583-590.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 583-590
    • Mende, K.1    Petoukhova, O.2    Koulitchkova, V.3    Schaub, G.A.4    Lange, U.5    Kaufmann, R.6    Nowak, G.7
  • 40
    • 0035942306 scopus 로고    scopus 로고
    • Electrostatic steering and ionic tethering in the formation of thrombin-hirudin complexes: The role of the thrombin anion-binding exosite- I
    • Myles, T., Le Bonniec, B.F., Betz, A., Stone, S.R., 2001. Electrostatic steering and ionic tethering in the formation of thrombin-hirudin complexes: The role of the thrombin anion-binding exosite- I. Biochemistry 40, 4972-4979.
    • (2001) Biochemistry , vol.40 , pp. 4972-4979
    • Myles, T.1    Le Bonniec, B.F.2    Betz, A.3    Stone, S.R.4
  • 41
    • 0032887014 scopus 로고    scopus 로고
    • Savignin, a potent thrombin inhibitor isolated from the salivary glands of the tick Ornithodoros savignyi (Acari: Argasidae)
    • Nienaber, J., Gaspar, A.R., Neitz, A.W., 1999. Savignin, a potent thrombin inhibitor isolated from the salivary glands of the tick Ornithodoros savignyi (Acari: Argasidae). Exp. Parasitol. 93, 82-91.
    • (1999) Exp. Parasitol. , vol.93 , pp. 82-91
    • Nienaber, J.1    Gaspar, A.R.2    Neitz, A.W.3
  • 43
    • 28444470134 scopus 로고    scopus 로고
    • Determinants of specificity in coagulation proteases
    • Page, M.J., Macgillivray, R.T., Di Cera, E., 2005. Determinants of specificity in coagulation proteases. J. Thromb. Haemost. 3, 2401-2408.
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 2401-2408
    • Page, M.J.1    Macgillivray, R.T.2    Di Cera, E.3
  • 44
  • 45
    • 0029090233 scopus 로고
    • Blood-feeding arthropods: Live syringes or invertebrate pharmacologists?
    • Ribeiro, J.M., 1995. Blood-feeding arthropods: live syringes or invertebrate pharmacologists? Infect. Agents Dis. 4, 143-152.
    • (1995) Infect. Agents Dis. , vol.4 , pp. 143-152
    • Ribeiro, J.M.1
  • 46
    • 0037208861 scopus 로고    scopus 로고
    • Role of arthropod saliva in blood feeding: Sialome and post-sialome perspectives
    • Ribeiro, J.M., Francischetti, I.M., 2003. Role of arthropod saliva in blood feeding: sialome and post-sialome perspectives. Annu. Rev. Entomol. 48, 73-88.
    • (2003) Annu. Rev. Entomol. , vol.48 , pp. 73-88
    • Ribeiro, J.M.1    Francischetti, I.M.2
  • 47
    • 0037176829 scopus 로고    scopus 로고
    • Characterization of the residues involved in the human α-thrombin-haemadin complex: An exosite II-binding inhibitor
    • Richardson, J.L., Fuentes-Prior, P., Sadler, J.E., Huber, R., Bode, W., 2002. Characterization of the residues involved in the human α-thrombin-haemadin complex: An exosite II-binding inhibitor. Biochemistry 41, 2535-2542.
    • (2002) Biochemistry , vol.41 , pp. 2535-2542
    • Richardson, J.L.1    Fuentes-Prior, P.2    Sadler, J.E.3    Huber, R.4    Bode, W.5
  • 50
    • 0025866812 scopus 로고
    • Refined structure of the hirudin-thrombin complex
    • Rydel, T.J., Tulinsky, A., Bode, W., Huber, R., 1991. Refined structure of the hirudin-thrombin complex. J. Mol. Biol. 221, 583-601.
    • (1991) J. Mol. Biol. , vol.221 , pp. 583-601
    • Rydel, T.J.1    Tulinsky, A.2    Bode, W.3    Huber, R.4
  • 51
    • 0027287309 scopus 로고
    • Novel hirudin variants from the leech Hirudinaria manillensis. Amino acid sequence, cDNA cloning and genomic organization
    • Scacheri, E., Nitti, G., Valsasina, B., Orsini, G., Visco, C., Ferrera, M., Sawyer, R.T., Sarmientos, P., 1993. Novel hirudin variants from the leech Hirudinaria manillensis. Amino acid sequence, cDNA cloning and genomic organization. Eur. J. Biochem. 214, 295-304.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 295-304
    • Scacheri, E.1    Nitti, G.2    Valsasina, B.3    Orsini, G.4    Visco, C.5    Ferrera, M.6    Sawyer, R.T.7    Sarmientos, P.8
  • 52
    • 0024465384 scopus 로고
    • Primary structures of new 'iso-hirudins'
    • Scharf, M., Engels, J., Tripier, D., 1989. Primary structures of new 'iso-hirudins'. FEBS Lett. 255, 105-110.
    • (1989) FEBS Lett , vol.255 , pp. 105-110
    • Scharf, M.1    Engels, J.2    Tripier, D.3
  • 55
    • 0022521744 scopus 로고
    • Kinetics of the inhibition of thrombin by hirudin
    • Stone, S.R., Hofsteenge, J., 1986. Kinetics of the inhibition of thrombin by hirudin. Biochemistry 25, 4622-4628.
    • (1986) Biochemistry , vol.25 , pp. 4622-4628
    • Stone, S.R.1    Hofsteenge, J.2
  • 56
    • 0027516408 scopus 로고
    • Isolation, sequence analysis, and cloning of haemadin. An anticoagulant peptide from the Indian leech
    • Strube, K.H., Kroger, B., Bialojan, S., Otte, M., Dodt, J., 1993. Isolation, sequence analysis, and cloning of haemadin. An anticoagulant peptide from the Indian leech. J. Biol. Chem. 268, 8590-8595.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8590-8595
    • Strube, K.H.1    Kroger, B.2    Bialojan, S.3    Otte, M.4    Dodt, J.5
  • 57
    • 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., Huber, R., Friedrich, T., Kroger, B., Hoffken, W., Bode, W., 1995. Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin. EMBO J. 14, 5149-5157.
    • (1995) EMBO J , vol.14 , pp. 5149-5157
    • Van De Locht, A.1    Lamba, D.2    Bauer, M.3    Huber, R.4    Friedrich, T.5    Kroger, B.6    Hoffken, W.7    Bode, W.8
  • 60
    • 0024835297 scopus 로고
    • Contribution of the N-terminal region of hirudin to its interaction with thrombin
    • Wallace, A., Dennis, S., Hofsteenge, J., Stone, S.R., 1989. Contribution of the N-terminal region of hirudin to its interaction with thrombin. Biochemistry 28, 10079-10084.
    • (1989) Biochemistry , vol.28 , pp. 10079-10084
    • Wallace, A.1    Dennis, S.2    Hofsteenge, J.3    Stone, S.R.4
  • 62
    • 0032575297 scopus 로고    scopus 로고
    • Nitrophorin-2: A novel mixed-type reversible specific inhibitor of the intrinsic factor-X activating complex
    • Zhang, Y., Ribeiro, J.M., Guimaraes, J.A., Walsh, P.N., 1998. Nitrophorin-2: A novel mixed-type reversible specific inhibitor of the intrinsic factor-X activating complex. Biochemistry 37, 10681-10690.
    • (1998) Biochemistry , vol.37 , pp. 10681-10690
    • Zhang, Y.1    Ribeiro, J.M.2    Guimaraes, J.A.3    Walsh, P.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.