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Volumn 80, Issue 4, 2003, Pages 451-462

Directed evolution towards protease-resistant hirudin variants

Author keywords

Directed evolution; Hirudin; Phage display; Protease resistance; Thrombin inhibitor design

Indexed keywords

ASPARTIC ACID; CHYMOTRYPSIN; HISTIDINE; PEPSIN A; POLYPEPTIDE; PROLINE; PROTEINASE; RECOMBINANT HIRUDIN; THROMBIN; THROMBIN INHIBITOR;

EID: 0344493788     PISSN: 10967192     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ymgme.2003.09.007     Document Type: Article
Times cited : (9)

References (39)
  • 1
    • 0000019735 scopus 로고
    • Die Isolierung und chemische Charakterisierung des Hirudins
    • Markwardt F. Die Isolierung und chemische Charakterisierung des Hirudins. Hoppe-Seyler's Z. Physiol. Chem. 308:1957;147-156.
    • (1957) Hoppe-Seyler's Z. Physiol. Chem. , vol.308 , pp. 147-156
    • Markwardt, F.1
  • 2
    • 0001918129 scopus 로고
    • Ligand binding: Proteinase-protein inhibitor interactions
    • Bode W., Huber R. Ligand binding: proteinase-protein inhibitor interactions. Curr. Opin. Struct. Biol. 1:1991;45-52.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 45-52
    • Bode, W.1    Huber, R.2
  • 3
    • 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. Use of site-directed mutagenesis to investigate the basis for the specificity of hirudin. Biochemistry. 27:1988;6517-6522.
    • (1988) Biochemistry , vol.27 , pp. 6517-6522
    • Braun, P.J.1    Dennis, S.2    Hofsteenge, J.3    Stone, S.R.4
  • 4
    • 0025614350 scopus 로고
    • Production, properties, and thrombin inhibitory mechanism of hirudin amino-terminal core fragments
    • Chang J.-Y. Production, properties, and thrombin inhibitory mechanism of hirudin amino-terminal core fragments. J. Biol. Chem. 265:1990;22159-22166.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22159-22166
    • Chang, J.-Y.1
  • 5
    • 0024536148 scopus 로고
    • Point mutations modifying the thrombin inhibition kinetics and antithrombotic activity in vivo of recombinant hirudin
    • Degryse E., Acker M., Defreyn G., Bernat A., Maffrand J.P., Roitsch C., Courtney M. Point mutations modifying the thrombin inhibition kinetics and antithrombotic activity in vivo of recombinant hirudin. Protein Eng. 2:1989;459-465.
    • (1989) Protein Eng. , vol.2 , pp. 459-465
    • Degryse, E.1    Acker, M.2    Defreyn, G.3    Bernat, A.4    Maffrand, J.P.5    Roitsch, C.6    Courtney, M.7
  • 6
    • 0023841705 scopus 로고
    • Interaction of site specific hirudin variants with α-thrombin
    • Dodt J., Köhler S., Baici A. Interaction of site specific hirudin variants with α-thrombin. FEBS Lett. 229:1988;87-90.
    • (1988) FEBS Lett. , vol.229 , pp. 87-90
    • Dodt, J.1    Köhler, S.2    Baici, A.3
  • 7
    • 0025346345 scopus 로고
    • Design and characterization of hirulogs: A novel class of bivalent peptide inhibitors of thrombin
    • Maraganore J.M., Bourdon P., Jablonski K.L., Ramachandran K.L., FentonII J.W. Design and characterization of hirulogs: a novel class of bivalent peptide inhibitors of thrombin. Biochemistry. 29:1990;7095-7101.
    • (1990) Biochemistry , vol.29 , pp. 7095-7101
    • Maraganore, J.M.1    Bourdon, P.2    Jablonski, K.L.3    Ramachandran, K.L.4    Fentonii, J.W.5
  • 8
    • 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. Contribution of the N-terminal region of hirudin to its interaction with thrombin. Biochemistry. 28:1989;10079-10084.
    • (1989) Biochemistry , vol.28 , pp. 10079-10084
    • Wallace, A.1    Dennis, S.2    Hofsteenge, J.3    Stone, S.R.4
  • 9
    • 0036353340 scopus 로고    scopus 로고
    • Modular design of a novel chimeric protein with combined thrombin inhibitory activity and plasminogen activating potential
    • Wirsching F., Luge C., Schwienhorst A. Modular design of a novel chimeric protein with combined thrombin inhibitory activity and plasminogen activating potential. Mol. Genet. Metab. 75:2002;250-259.
    • (2002) Mol. Genet. Metab. , vol.75 , pp. 250-259
    • Wirsching, F.1    Luge, C.2    Schwienhorst, A.3
  • 10
    • 0027960880 scopus 로고
    • Probing the structure of hirudin from Hirudinaria manillensis by limited proteolysis. Isolation, characterization and thrombin-inhibitory properties of N-terminal fragments
    • Vindigni A., De Filippis V., Zanotti G., Visco C., Orsini G., Fontana A. Probing the structure of hirudin from Hirudinaria manillensis by limited proteolysis. Isolation, characterization and thrombin-inhibitory properties of N-terminal fragments. Eur. J. Biochem. 226:1994;323-333.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 323-333
    • Vindigni, A.1    De Filippis, V.2    Zanotti, G.3    Visco, C.4    Orsini, G.5    Fontana, A.6
  • 13
    • 0023874875 scopus 로고
    • Pharmacokinetics and pharmacodynamics of hirudin in man after single subcutaneous and intravenous bolus administration
    • Bichler J., Fichtl B., Siebeck M., Fritz H. Pharmacokinetics and pharmacodynamics of hirudin in man after single subcutaneous and intravenous bolus administration. Arzeinm Forsch./Drug Res. 38:1988;704-710.
    • (1988) Arzeinm Forsch./Drug Res. , vol.38 , pp. 704-710
    • Bichler, J.1    Fichtl, B.2    Siebeck, M.3    Fritz, H.4
  • 15
    • 0028559927 scopus 로고
    • Design of potent bivalent thrombin inhibitors based on hirudin sequence: Incorporation of nonsubstrate-type active site inhibitors
    • Tsuda Y., Cygler M., Gibbs B.F., Pedyczak A., Féthière J., Yue S.Y., Konishi Y. Design of potent bivalent thrombin inhibitors based on hirudin sequence: incorporation of nonsubstrate-type active site inhibitors. Biochemistry. 33:1994;14443-14451.
    • (1994) Biochemistry , vol.33 , pp. 14443-14451
    • Tsuda, Y.1    Cygler, M.2    Gibbs, B.F.3    Pedyczak, A.4    Féthière, J.5    Yue, S.Y.6    Konishi, Y.7
  • 16
    • 0027765635 scopus 로고
    • Catabolism of hirudin and thrombin-hirudin complexes in the rat
    • Bichler J., Baynes J.W., Thorpe S.R. Catabolism of hirudin and thrombin-hirudin complexes in the rat. Biochem. J. 296:1993;771-776.
    • (1993) Biochem. J. , vol.296 , pp. 771-776
    • Bichler, J.1    Baynes, J.W.2    Thorpe, S.R.3
  • 18
  • 23
    • 0031578799 scopus 로고    scopus 로고
    • Display of functional thrombin inhibitor hirudin on the surface of phage M13
    • Wirsching F., Opitz T., Dietrich R., Schwienhorst A. Display of functional thrombin inhibitor hirudin on the surface of phage M13. Gene. 204:1997;177-184.
    • (1997) Gene , vol.204 , pp. 177-184
    • Wirsching, F.1    Opitz, T.2    Dietrich, R.3    Schwienhorst, A.4
  • 24
    • 0026786833 scopus 로고
    • Conformationally restricted thrombin inhibitors resistant to proteolytic digestion
    • Szewczuk Z., Gibbs B.F., Yue S.Y., Purisima E.O., Konishi Y. Conformationally restricted thrombin inhibitors resistant to proteolytic digestion. Biochemistry. 31:1992;9132-9140.
    • (1992) Biochemistry , vol.31 , pp. 9132-9140
    • Szewczuk, Z.1    Gibbs, B.F.2    Yue, S.Y.3    Purisima, E.O.4    Konishi, Y.5
  • 25
    • 0025866812 scopus 로고
    • Refined structure of the hirudin-thrombin complex
    • Rydel T.J., Tulinsky A., Bode W., Huber R. Refined structure of the hirudin-thrombin complex. JMB. 221:1991;583-601.
    • (1991) JMB , vol.221 , pp. 583-601
    • Rydel, T.J.1    Tulinsky, A.2    Bode, W.3    Huber, R.4
  • 26
    • 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. Interaction of the N-terminal region of hirudin with the active-site cleft of thrombin. Biochemistry. 31:1992;4557-4562.
    • (1992) Biochemistry , vol.31 , pp. 4557-4562
    • Betz, A.1    Hofsteenge, J.2    Stone, S.R.3
  • 27
    • 0024465384 scopus 로고
    • Primary structures of new 'iso-hirudins'
    • Scharf M., Engels J., Tripier D. Primary structures of new 'iso-hirudins'. FEBS Lett. 255:1989;105-110.
    • (1989) FEBS Lett. , vol.255 , pp. 105-110
    • Scharf, M.1    Engels, J.2    Tripier, D.3
  • 28
    • 85007266296 scopus 로고    scopus 로고
    • R. Maschler, V. Steiner, M.G. Grütter, R. Fritz, DNA vector and recombinant host cell for production of hirullin P6 and P18, Eur. Patent Application 89810414.6, EP-AP0347376, 1988
    • R. Maschler, V. Steiner, M.G. Grütter, R. Fritz, DNA vector and recombinant host cell for production of hirullin P6 and P18, Eur. Patent Application 89810414.6, EP-AP0347376, 1988.
  • 29
    • 0026102746 scopus 로고
    • Structure-function relationships of the C-terminal functional domain of hirudin and its variants
    • Krstenansky J.L., Mao S.J.T. Structure-function relationships of the C-terminal functional domain of hirudin and its variants. Blood Coagul. Fibrinolysis. 2:1991;91-96.
    • (1991) Blood Coagul. Fibrinolysis , vol.2 , pp. 91-96
    • Krstenansky, J.L.1    Mao, S.J.T.2
  • 30
    • 0026074854 scopus 로고
    • Hirudin: Amino-terminal residues play a major role in the interaction with thrombin
    • Lazar J.B., Winant R.C., Johnson P.H. Hirudin: amino-terminal residues play a major role in the interaction with thrombin. J. Biol. Chem. 266:1991;685-688.
    • (1991) J. Biol. Chem. , vol.266 , pp. 685-688
    • Lazar, J.B.1    Winant, R.C.2    Johnson, P.H.3
  • 31
    • 0037137217 scopus 로고    scopus 로고
    • Probing the hirudin-thrombin interaction by incorporation of noncoded amino acids and molecular dynamics simulation
    • De Filippis V., Colombo G., Russo I., Spadari B., Fontana A. Probing the hirudin-thrombin interaction by incorporation of noncoded amino acids and molecular dynamics simulation. Biochemistry. 41:2002;13556-13569.
    • (2002) Biochemistry , vol.41 , pp. 13556-13569
    • De Filippis, V.1    Colombo, G.2    Russo, I.3    Spadari, B.4    Fontana, A.5
  • 33
    • 0024284197 scopus 로고
    • The AGG codon is translated slowly in E. coli even at very low expression levels
    • Bonekamp F., Jensen K.F. The AGG codon is translated slowly in E. coli even at very low expression levels. NAR. 16:1988;3013-3024.
    • (1988) NAR , vol.16 , pp. 3013-3024
    • Bonekamp, F.1    Jensen, K.F.2
  • 34
    • 0024825088 scopus 로고
    • High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product
    • Brinkmann U., Mattes R.E., Buckel P. High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product. Gene. 85:1989;109-114.
    • (1989) Gene , vol.85 , pp. 109-114
    • Brinkmann, U.1    Mattes, R.E.2    Buckel, P.3
  • 37
    • 0025338124 scopus 로고
    • Thrombin-bound conformation of the C-terminal fragmens of hirudin determined by transferred nuclear overhauser effects
    • Ni F., Konishi Y., Scheraga H.A. Thrombin-bound conformation of the C-terminal fragmens of hirudin determined by transferred nuclear overhauser effects. Biochemistry. 29:1990;4479-4489.
    • (1990) Biochemistry , vol.29 , pp. 4479-4489
    • Ni, F.1    Konishi, Y.2    Scheraga, H.A.3
  • 38
    • 0028349915 scopus 로고
    • Mapping of the thrombin des-ETW conformation by using site-directed mutants of hirudin. Evidence for the induction of nonlocal modifications by mutagenesis
    • LeBonniec B.F., Betz A., Guinto E.R., Esmon C.T., Stone S.R. Mapping of the thrombin des-ETW conformation by using site-directed mutants of hirudin. Evidence for the induction of nonlocal modifications by mutagenesis. Biochemistry. 33:1994;3959-3966.
    • (1994) Biochemistry , vol.33 , pp. 3959-3966
    • Lebonniec, B.F.1    Betz, A.2    Guinto, E.R.3    Esmon, C.T.4    Stone, S.R.5
  • 39
    • 0021689983 scopus 로고
    • Conformational specificity of chymotrypsin toward proline-containing substrates
    • Fischer G., Bang H., Berger E., Schellenberger A. Conformational specificity of chymotrypsin toward proline-containing substrates. Biochim. Biophys. Acta. 79:1984;87-97.
    • (1984) Biochim. Biophys. Acta , vol.79 , pp. 87-97
    • Fischer, G.1    Bang, H.2    Berger, E.3    Schellenberger, A.4


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