메뉴 건너뛰기




Volumn 76, Issue 2-3, 1998, Pages 177-188

NMR for the design of functional mimetics of protein-protein interactions: One key is in the building of bridges

Author keywords

Bridge binding inhibitors; Functional mimetics; NMR; Protein protein interactions; Thrombin

Indexed keywords

HIRUDIN; THROMBIN;

EID: 0032467377     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o98-046     Document Type: Review
Times cited : (34)

References (67)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Washington, D.C.
    • Anfinsen, C.B. 1973. Principles that govern the folding of protein chains. Science (Washington, D.C.), 181: 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0027268487 scopus 로고
    • Design of peptide enzymes (pepzymes): Surface-simulation synthetic peptides that mimic the chymotrypsin and trypsin active sites and exhibit the activity and specificity of the respective enzyme
    • Atassi, M.Z., and Manshouri, T. 1993. Design of peptide enzymes (pepzymes): surface-simulation synthetic peptides that mimic the chymotrypsin and trypsin active sites and exhibit the activity and specificity of the respective enzyme. Proc. Natl. Acad. Sci. U.S.A. 90: 8282-8286.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 8282-8286
    • Atassi, M.Z.1    Manshouri, T.2
  • 4
    • 0015530781 scopus 로고
    • Negative nuclear Overhauser effects as probes of macromolecular structure
    • Balaram, P., Bothner-By, A.A., and Dadok, J. 1972a. Negative nuclear Overhauser effects as probes of macromolecular structure. J. Am. Chem. Soc. 94: 4015-4017.
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 4015-4017
    • Balaram, P.1    Bothner-By, A.A.2    Dadok, J.3
  • 5
    • 0015530821 scopus 로고
    • Localization of tyrosine at binding of neurophysin II by negative nuclear Overhauser effects
    • Balaram, P., Bothner-By, A.A., and Dadok, J. 1972b. Localization of tyrosine at binding of neurophysin II by negative nuclear Overhauser effects. J. Am. Chem. Soc. 94: 4017-4018.
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 4017-4018
    • Balaram, P.1    Bothner-By, A.A.2    Dadok, J.3
  • 7
    • 0013623040 scopus 로고
    • Substrate specificity of thrombin on proteins and synthetic subtrates
    • Edited by R. Lundblad and K.G. Mann. Ann Arbor Science Press, Ann Arbor, Mich
    • Blombäck, B., Hessel, B., Hogg, D., and Claesson, G. 1977. Substrate specificity of thrombin on proteins and synthetic subtrates. In Chemistry and biology of thrombin. Edited by R. Lundblad and K.G. Mann. Ann Arbor Science Press, Ann Arbor, Mich. pp. 275-290.
    • (1977) Chemistry and Biology of Thrombin , pp. 275-290
    • Blombäck, B.1    Hessel, B.2    Hogg, D.3    Claesson, G.4
  • 8
    • 0029904435 scopus 로고    scopus 로고
    • Minimizing a binding domain from protein A
    • Braisted, A., and Wells, J.A. 1996. Minimizing a binding domain from protein A. Proc. Natl. Acad. Sci. U.S.A. 93: 5688-5692.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5688-5692
    • Braisted, A.1    Wells, J.A.2
  • 9
    • 0023766115 scopus 로고
    • Use of site-directed mutagenesis to investigate the basis for the specificity of hirudin
    • Braun, P.J., Dennis, S., Hofsteenge, J., and 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
  • 10
    • 0027215829 scopus 로고
    • The two-dimensional transferred nuclear Overhauser effect: Theory and practice
    • Campbell, A.P., and Sykes, B.D. 1993. The two-dimensional transferred nuclear Overhauser effect: theory and practice. Annu. Rev. Biophys. Biomol. Struct. 22: 99-122.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 99-122
    • Campbell, A.P.1    Sykes, B.D.2
  • 11
    • 0021024613 scopus 로고
    • The functional domain of hirudin, α thrombin-specific inhibitor
    • Chang, J.Y. 1983. The functional domain of hirudin, α thrombin-specific inhibitor. FEBS Lett. 164: 307-313.
    • (1983) FEBS Lett. , vol.164 , pp. 307-313
    • Chang, J.Y.1
  • 12
    • 0024514373 scopus 로고
    • The hirudin-binding site of human α-thrombin
    • Chang, J.Y. 1989. The hirudin-binding site of human α-thrombin. J. Biol. Chem. 264: 7141-7146.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7141-7146
    • Chang, J.Y.1
  • 13
    • 0025141415 scopus 로고
    • Antithrombin activity of the hirudin N-terminal core domain residues 1-43
    • Chang, J.Y., Schlaeppi, J.M., and Stone, S.R. 1990. Antithrombin activity of the hirudin N-terminal core domain residues 1-43. FEBS Lett. 260: 209-212.
    • (1990) FEBS Lett. , vol.260 , pp. 209-212
    • Chang, J.Y.1    Schlaeppi, J.M.2    Stone, S.R.3
  • 14
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Washington, D.C.
    • Clackson, T., and Wells, J.A. 1995. A hot spot of binding energy in a hormone-receptor interface. Science (Washington, D.C.), 267: 383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 16
    • 0024403619 scopus 로고
    • High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis
    • Washington, D.C.
    • Cunningham, B.C., and Wells, J.A. 1989. High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science (Washington, D.C.), 244: 1081-1085.
    • (1989) Science , vol.244 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 19
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • Washington, D.C.
    • de Vos, A.M., Ultsch, A.A., and Kossiakoff, A.A. 1992. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science (Washington, D.C.), 255: 306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, A.A.2    Kossiakoff, A.A.3
  • 20
    • 0025674180 scopus 로고
    • Bifunctional thrombin inhibitors based on the sequence of hirudin
    • DiMaio, J., Gibbs, B., Munn, D., Lefebvre, J., Ni, F., and Konishi, Y 1990. Bifunctional thrombin inhibitors based on the sequence of hirudin. J. Biol. Chem. 265: 21698-21703.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21698-21703
    • DiMaio, J.1    Gibbs, B.2    Munn, D.3    Lefebvre, J.4    Ni, F.5    Konishi, Y.6
  • 21
    • 0025906031 scopus 로고
    • A new class of potent thrombin inhibitors that incorporate a scissile pseudopeptide bond
    • DiMaio, J., Ni, F., Gibbs, B., and Konishi, Y. 1991. A new class of potent thrombin inhibitors that incorporate a scissile pseudopeptide bond. FEBS Lett. 287: 47-52.
    • (1991) FEBS Lett. , vol.287 , pp. 47-52
    • DiMaio, J.1    Ni, F.2    Gibbs, B.3    Konishi, Y.4
  • 23
    • 0021331392 scopus 로고
    • The complete amino acid sequence of hirudin, a thrombin specific inhibitor
    • Dodt, J., Muller, H.P., Seemüller, U., and Chang, J.Y. 1984. The complete amino acid sequence of hirudin, a thrombin specific inhibitor. FEBS Lett 165: 180-183.
    • (1984) FEBS Lett , vol.165 , pp. 180-183
    • Dodt, J.1    Muller, H.P.2    Seemüller, U.3    Chang, J.Y.4
  • 24
    • 0019729451 scopus 로고
    • Thrombin specificity
    • Fenton, J.W., II. 1981. Thrombin specificity. Ann. N.Y. Acad. Sci. 370: 468-495.
    • (1981) Ann. N.Y. Acad. Sci. , vol.370 , pp. 468-495
    • Fenton J.W. II1
  • 25
    • 0026102830 scopus 로고
    • Thrombin structure and function: Why thrombin is the primary target for antithrombotics
    • Fenton, J.W., II, Ofosu, F.A., Moon, D.G., and Maraganore, J.M. 1991. Thrombin structure and function: why thrombin is the primary target for antithrombotics. Blood Coagul. Fibrinolysis, 2: 69-75.
    • (1991) Blood Coagul. Fibrinolysis , vol.2 , pp. 69-75
    • Fenton J.W. II1    Ofosu, F.A.2    Moon, D.G.3    Maraganore, J.M.4
  • 27
    • 0024498476 scopus 로고
    • Solution structure of recombinant hirudin and the Lys-47-Glu mutant: A nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study
    • Folkers, P.J., Clore, G.M., Driscoll, P.C., Dodt, J., Kohler, S., and Gronenborn, A.M. 1989. Solution structure of recombinant hirudin and the Lys-47-Glu mutant: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study. Biochemistry, 28: 601-617.
    • (1989) Biochemistry , vol.28 , pp. 601-617
    • Folkers, P.J.1    Clore, G.M.2    Driscoll, P.C.3    Dodt, J.4    Kohler, S.5    Gronenborn, A.M.6
  • 29
    • 0024403533 scopus 로고
    • Conformation of recombinant desulfatohirudin in aqueous solution determined by nuclear magnetic resonance
    • Haruyama, H., and Wüthrich, 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    Wüthrich, K.2
  • 31
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin, J., and Chothia, C. 1990. The structure of protein-protein recognition sites. J. Biol. Chem. 265: 16027-16030.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 32
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks, W.P. 1981. On the attribution and additivity of binding energies. Proc. Natl. Acad. Sci. U.S.A. 78: 4046-4050.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 33
    • 0018750813 scopus 로고
    • D-Phe-Pro-ArgCH2C1-A selective affinity label for thrombin Thromb
    • Kettner, C., and Shaw, E. 1979. D-Phe-Pro-ArgCH2C1-A selective affinity label for thrombin Thromb. Res. 14: 969-973.
    • (1979) Res. , vol.14 , pp. 969-973
    • Kettner, C.1    Shaw, E.2
  • 34
    • 0029879577 scopus 로고    scopus 로고
    • Synthesis, structure, and structure-activity relationships of divalent thrombin inhibitors containing an α-keto-amide transition-state mimetic
    • Krishnan, R., Tulinsky, A., Vlasuk, G.P., Pearson, D., Vallar, P., Bergum, P., Brunck, T.K., and Ripka, W.C. 1996. Synthesis, structure, and structure-activity relationships of divalent thrombin inhibitors containing an α-keto-amide transition-state mimetic. Protein Sci. 5: 422-433.
    • (1996) Protein Sci. , vol.5 , pp. 422-433
    • Krishnan, R.1    Tulinsky, A.2    Vlasuk, G.P.3    Pearson, D.4    Vallar, P.5    Bergum, P.6    Brunck, T.K.7    Ripka, W.C.8
  • 35
    • 0018886368 scopus 로고
    • Studies on synthetic peptides that bind to fibrinogen and prevent fibrin polymerization. Structural requirements, number of binding sites, and species differences
    • Laudano, A.P., and Doolittle, R.F. 1980. Studies on synthetic peptides that bind to fibrinogen and prevent fibrin polymerization. Structural requirements, number of binding sites, and species differences. Biochemistry, 19: 1013-1019.
    • (1980) Biochemistry , vol.19 , pp. 1013-1019
    • Laudano, A.P.1    Doolittle, R.F.2
  • 37
    • 0025346345 scopus 로고
    • Design and characterization of hirulogs: A novel class of bivalent peptide inhibitors of thrombin
    • Maraganore, J.M., Bowidon, P., Jablonski, J., Ramacandran, K.L., and Fenton, J.W., II. 1990. Design and characterization of hirulogs: a novel class of bivalent peptide inhibitors of thrombin. Biochemistry, 29: 7095-7101.
    • (1990) Biochemistry , vol.29 , pp. 7095-7101
    • Maraganore, J.M.1    Bowidon, P.2    Jablonski, J.3    Ramacandran, K.L.4    Fenton J.W. II5
  • 38
    • 0019953798 scopus 로고
    • Pharmacological studies on the antithrombotic action of hirudin in experimental animals
    • Markwardt, F., Hauptmann, J., Nowak, G., Klessen, C., and Walsmann, P. 1982. Pharmacological studies on the antithrombotic action of hirudin in experimental animals. Thromb. Haemostasis, 47: 226-229.
    • (1982) Thromb. Haemostasis , vol.47 , pp. 226-229
    • Markwardt, F.1    Hauptmann, J.2    Nowak, G.3    Klessen, C.4    Walsmann, P.5
  • 40
    • 0028728698 scopus 로고
    • Recent developments in transferred NOE methods
    • Ni, F. 1994. Recent developments in transferred NOE methods. Prog. Nucl. Magn. Reson. Spectrosc. 26: 517-606.
    • (1994) Prog. Nucl. Magn. Reson. Spectrosc. , vol.26 , pp. 517-606
    • Ni, F.1
  • 41
    • 0023919814 scopus 로고
    • High-resolution NMR studies of fibrinogen-like peptides in solution: Resonance assignments and conformational analysis of residues 1-23 of the Aα chain of human fibrinogen
    • Ni, F., Lord, S.T., and Scheraga, A. 1988. High-resolution NMR studies of fibrinogen-like peptides in solution: resonance assignments and conformational analysis of residues 1-23 of the Aα chain of human fibrinogen. Biochemistry, 27: 4481-4491.
    • (1988) Biochemistry , vol.27 , pp. 4481-4491
    • Ni, F.1    Lord, S.T.2    Scheraga, A.3
  • 42
    • 12044258461 scopus 로고
    • Use of the transferred nuclear Overhauser effect to determine the conformations of ligands bound to protein
    • Ni, F., and Scheraga, H.A. 1994. Use of the transferred nuclear Overhauser effect to determine the conformations of ligands bound to protein. Acc. Chem. Res. 27: 257-264.
    • (1994) Acc. Chem. Res. , vol.27 , pp. 257-264
    • Ni, F.1    Scheraga, H.A.2
  • 43
    • 0024550340 scopus 로고
    • High-resolution NMR studies of fibrinogen-like peptides in solution: Interaction of thrombin with residues 1-23 of the A α chain of human fibrinogen
    • Ni, F., Konishi, Y., Frazier, R.B., Lord, S.T., and Scheraga, H.A. 1989a. High-resolution NMR studies of fibrinogen-like peptides in solution: interaction of thrombin with residues 1-23 of the A α chain of human fibrinogen. Biochemistry, 28: 3082-3094.
    • (1989) Biochemistry , vol.28 , pp. 3082-3094
    • Ni, F.1    Konishi, Y.2    Frazier, R.B.3    Lord, S.T.4    Scheraga, H.A.5
  • 44
    • 0024544276 scopus 로고
    • High-resolution NMR studies of fibrinogen-like peptides in solution: Structure of a thrombin-bound peptide corresponding to residues 7-16 of the Aα chain of human fibrinogen
    • Ni, F., Konishi, Y., Frazier, R.B., Lord, S.T., and Scheraga, H.A. 1989b. High-resolution NMR studies of fibrinogen-like peptides in solution: structure of a thrombin-bound peptide corresponding to residues 7-16 of the Aα chain of human fibrinogen. Biochemistry, 28: 3094-3105.
    • (1989) Biochemistry , vol.28 , pp. 3094-3105
    • Ni, F.1    Konishi, Y.2    Frazier, R.B.3    Lord, S.T.4    Scheraga, H.A.5
  • 45
    • 0024521572 scopus 로고
    • High-resolution NMR studies of fibrinogen-like peptides in solution: Structural basis for the bleeding disorder caused by a single mutation of Gly(12) to Val(12) in the Aα chain of human fibrinogen Rouen
    • Ni, F., Konishi, Y., Frazier, R.B., Lord, S.T., and Scheraga, H.A. 1989c. High-resolution NMR studies of fibrinogen-like peptides in solution: structural basis for the bleeding disorder caused by a single mutation of Gly(12) to Val(12) in the Aα chain of human fibrinogen Rouen. Biochemistry, 28: 3094-3105.
    • (1989) Biochemistry , vol.28 , pp. 3094-3105
    • Ni, F.1    Konishi, Y.2    Frazier, R.B.3    Lord, S.T.4    Scheraga, H.A.5
  • 46
    • 0025338124 scopus 로고
    • Thrombin-bound conformation of the C-terminal fragments of hirudin determined by transferred nuclear Overhauser effects
    • Ni, F., Konishi, Y., and Scheraga, H.A. 1990. Thrombin-bound conformation of the C-terminal fragments of hirudin determined by transferred nuclear Overhauser effects. Biochemistry, 29: 4479-4489.
    • (1990) Biochemistry , vol.29 , pp. 4479-4489
    • Ni, F.1    Konishi, Y.2    Scheraga, H.A.3
  • 47
    • 0026459469 scopus 로고
    • Solution structure of a platelet receptor peptide bound to bovine a-thrombin
    • Ni, F., Ripoll, D.R., Martin, P.D., and Edwards, F.P. 1992a. Solution structure of a platelet receptor peptide bound to bovine a-thrombin. Biochemistry, 31: 11551-11557.
    • (1992) Biochemistry , vol.31 , pp. 11551-11557
    • Ni, F.1    Ripoll, D.R.2    Martin, P.D.3    Edwards, F.P.4
  • 48
    • 0004167344 scopus 로고
    • Nuclear magnetic resonance studies of thrombin-fibrinopeptide and thrombin-hirudin complexes
    • Edited by L.J. Berliner. Plenum Press, New York
    • Ni, F., Gibson, K.D., and Scheraga, H.A. 1992b. Nuclear magnetic resonance studies of thrombin-fibrinopeptide and thrombin-hirudin complexes. In Thrombin: structure and function. Edited by L.J. Berliner. Plenum Press, New York. pp. 63-85.
    • (1992) Thrombin: Structure and Function , pp. 63-85
    • Ni, F.1    Gibson, K.D.2    Scheraga, H.A.3
  • 49
    • 0027274612 scopus 로고
    • Thrombin exosite for fibrinogen recognition is partially accessible in prothrombin
    • Ni, F., Ning, Q., Jackson, M.J., and Fenton, J.W., II. 1993. Thrombin exosite for fibrinogen recognition is partially accessible in prothrombin. J. Biol. Chem. 268: 16899-16902.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16899-16902
    • Ni, F.1    Ning, Q.2    Jackson, M.J.3    Fenton, J.W.4
  • 50
    • 0029151607 scopus 로고
    • Thrombin-bound structures of designed analogies of human fibrinopeptide A determined by quantitative transferred NOE spectroscopy: A new structural basis for thrombin specificity
    • Ni, F., Zhu, Y., and Scheraga, A. 1995. Thrombin-bound structures of designed analogies of human fibrinopeptide A determined by quantitative transferred NOE spectroscopy: a new structural basis for thrombin specificity. J. Mol. Biol. 252: 656-671.
    • (1995) J. Mol. Biol. , vol.252 , pp. 656-671
    • Ni, F.1    Zhu, Y.2    Scheraga, A.3
  • 51
    • 0028166473 scopus 로고
    • Thrombin-bound conformation of a cyclic anticoagulant peptide using transferred nuclear Overhauser effect (NOE), distance geometry, and NOE simulations
    • Ning, Q., Ripoll, D.R., Szewczuk, Z., Konishi, Y., and Ni, F. 1994. Thrombin-bound conformation of a cyclic anticoagulant peptide using transferred nuclear Overhauser effect (NOE), distance geometry, and NOE simulations. Biopolymers, 34: 1125-1137.
    • (1994) Biopolymers , vol.34 , pp. 1125-1137
    • Ning, Q.1    Ripoll, D.R.2    Szewczuk, Z.3    Konishi, Y.4    Ni, F.5
  • 52
    • 0024362070 scopus 로고
    • On the attribution of binding energy in antigen-antibody complexes McPC 603, D1.3, and HyHEL-5
    • Novotny, J., Bruccoleri, R.E., and Saul, F.A. 1989. On the attribution of binding energy in antigen-antibody complexes McPC 603, D1.3, and HyHEL-5. Biochemistry, 28: 4735-4749.
    • (1989) Biochemistry , vol.28 , pp. 4735-4749
    • Novotny, J.1    Bruccoleri, R.E.2    Saul, F.A.3
  • 54
    • 0027361390 scopus 로고
    • Experimental NMR techniques for studies of protein-ligand interactions
    • Otting, G. 1993. Experimental NMR techniques for studies of protein-ligand interactions. Curr. Opin. Struct. Biol. 3: 760.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 760
    • Otting, G.1
  • 55
    • 0025329390 scopus 로고
    • The structure of a complex of recombinant hirudin and human α-thrombin
    • Washington, D.C.
    • Rydel, T.J., Ravichandran, K.G., Tulinsky, A., Bode, W., Huber, R., Rottsch, C., and Fenton, J.W., II. 1990. The structure of a complex of recombinant hirudin and human α-thrombin. Science (Washington, D.C.), 249: 277-280.
    • (1990) Science , vol.249 , pp. 277-280
    • Rydel, T.J.1    Ravichandran, K.G.2    Tulinsky, A.3    Bode, W.4    Huber, R.5    Rottsch, C.6    Fenton J.W. II7
  • 56
    • 0022924075 scopus 로고
    • Chemical basis of thrombin interactions with fibrinogen
    • Scheraga, H.A. 1986. Chemical basis of thrombin interactions with fibrinogen. Ann. N.Y. Acad. Sci. 485: 124-133.
    • (1986) Ann. N.Y. Acad. Sci. , vol.485 , pp. 124-133
    • Scheraga, H.A.1
  • 57
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Washington, D.C.
    • Shuker, S.B., Hajduk, P.J., Meadows, R.P., and Fesik, S.W. 1996. Discovering high-affinity ligands for proteins: SAR by NMR. Science (Washington, D.C.), 274: 1531-1534.
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 58
    • 0023279803 scopus 로고
    • Identification of regions of alpha-thrombin involved in its interaction with hirudin
    • Stone, S.R., Braun, P.J., and Hofsteenge, J. 1987. Identification of regions of alpha-thrombin involved in its interaction with hirudin. Biochemistry, 26: 4617-4624.
    • (1987) Biochemistry , vol.26 , pp. 4617-4624
    • Stone, S.R.1    Braun, P.J.2    Hofsteenge, J.3
  • 59
    • 0015465694 scopus 로고
    • Substrates for determination of trypsin, thrombin and thrombin-like enzymes
    • Svendsen, L., Blombäck, B., Blombäk, M., and Olsson, P.I. 1972. Substrates for determination of trypsin, thrombin and thrombin-like enzymes. Folia Haematol. (Leipzig), 98: 446-454.
    • (1972) Folia Haematol. (Leipzig) , vol.98 , pp. 446-454
    • Svendsen, L.1    Blombäck, B.2    Blombäk, M.3    Olsson, P.I.4
  • 60
    • 0026786833 scopus 로고
    • Conformational restricted thrombin inhibitors resistant to protelytic digestion
    • Szewczuk, Z., Gibbs, B.F., Yue, S.Y., Purisima, E.O., and Konishi, Y. 1992. Conformational restricted thrombin inhibitors resistant to protelytic digestion. Biochemistry, 31: 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
  • 61
    • 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., Friedrick, T., Kroger, B., Hoffken, W., and 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    Friedrick, T.5    Kroger, B.6    Hoffken, W.7    Bode, W.8
  • 65
    • 0026502889 scopus 로고
    • Characterization of the interactions of a bifunctional inhibitor with α-thrombin by molecular modelling and peptide synthesis
    • Yue, S.Y., DiMaio, J., Szewczuk, Z., Purisima, E.O., Ni, F., and Konishi, Y. 1992. Characterization of the interactions of a bifunctional inhibitor with α-thrombin by molecular modelling and peptide synthesis. Protein Eng. 5: 77-85.
    • (1992) Protein Eng. , vol.5 , pp. 77-85
    • Yue, S.Y.1    DiMaio, J.2    Szewczuk, Z.3    Purisima, E.O.4    Ni, F.5    Konishi, Y.6
  • 66
  • 67
    • 0026635368 scopus 로고
    • Thrombin hydrolysis of an N-terminal peptide from fibrinogen lille: Kinetic and NMR studies
    • Zheng, Z., Ashton, R.W., Ni, F., and Scheraga, H.A. 1992. Thrombin hydrolysis of an N-terminal peptide from fibrinogen Lille: kinetic and NMR studies. Biochemistry, 31: 4426-4431.
    • (1992) Biochemistry , vol.31 , pp. 4426-4431
    • Zheng, Z.1    Ashton, R.W.2    Ni, F.3    Scheraga, H.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.