메뉴 건너뛰기




Volumn 41, Issue 13, 1998, Pages 2289-2301

Synthesis and evaluation of diphenyl phosphonate esters as inhibitors of the trypsin-like granzymes A and K and mast cell tryptase

Author keywords

[No Author keywords available]

Indexed keywords

DIPHENYL N (N BENZYLOXYCARBONBNYLALANYL)AMINO (4 AMIDINOPHENYL)METHANEPHOSPHONATE; DIPHENYL N (N BENZYLOXYCARBONYLALANYLALANYLALANYL)AMINO (4 AMIDINOPHENYL)METHANEPHOSPHONATE; DIPHENYL N (N SUCCINYLALANYLALANYL)AMINO (4 AMIDINOPHENYL)METHANEPHOSPHONATE; ENZYME INHIBITOR; GRANZYME A; GRANZYME A INHIBITOR; GRANZYME K INHIBITOR; TRYPTASE; TRYPTASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 0032543521     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm970543s     Document Type: Article
Times cited : (59)

References (59)
  • 1
    • 0020643008 scopus 로고
    • Cytotoxic T-Lymphocytes: How do they Function?
    • 2(2) Berke, G. Cytotoxic T-Lymphocytes: How do they Function? Immunol. Rev. 1983, 72, 5-38.
    • (1983) Immunol. Rev. , vol.72 , pp. 5-38
    • Berke, G.1
  • 2
    • 0031053758 scopus 로고    scopus 로고
    • Killing Mechanisms of Cytotoxic Lymphocytes
    • Berke, G. Killing Mechanisms of Cytotoxic Lymphocytes. Curr. Opin. Hematol. 1997, 4, 32-40.
    • (1997) Curr. Opin. Hematol. , vol.4 , pp. 32-40
    • Berke, G.1
  • 3
    • 0021183979 scopus 로고
    • Cytolytic Activity of Purified Cytoplasmic Granules from Cytotoxic Rat Large Granular Lymphocyte Tumors
    • Henkart, P. A.; Millard, P. J.; Reynolds, C. W.; Henkart, M. P. Cytolytic Activity of Purified Cytoplasmic Granules from Cytotoxic Rat Large Granular Lymphocyte Tumors. J. Exp. Med. 1984, 160, 75-93.
    • (1984) J. Exp. Med. , vol.160 , pp. 75-93
    • Henkart, P.A.1    Millard, P.J.2    Reynolds, C.W.3    Henkart, M.P.4
  • 4
    • 0021270576 scopus 로고
    • Cytolytic T Cell Granules. Isolation, Structural, Biochemical, and Functional Characterization
    • Podack, E. R.; Konigsberg, P. J. Cytolytic T Cell Granules. Isolation, Structural, Biochemical, and Functional Characterization. J. Exp. Med. 1984, 160, 695-710.
    • (1984) J. Exp. Med. , vol.160 , pp. 695-710
    • Podack, E.R.1    Konigsberg, P.J.2
  • 5
    • 0022253052 scopus 로고
    • Isolation of Lytic, Pore-forming Protein (Perform) from Cytolytic T-Lymphocyte
    • Masson, D.; Tschopp, J. Isolation of Lytic, Pore-forming Protein (Perform) from Cytolytic T-Lymphocyte. J. Biol. Chem. 1985, 260, 9069-9072.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9069-9072
    • Masson, D.1    Tschopp, J.2
  • 6
    • 0001041396 scopus 로고
    • Isolation and Biochemical and Functional Characterization of Perform 1 from Cytolytic T-Cell Granules
    • Podack, E. R.; Young, J. D. E.; Cohn, Z. A. Isolation and Biochemical and Functional Characterization of Perform 1 from Cytolytic T-Cell Granules. Prod. Natl. Acad. Sci. U.S.A. 1985, 82, 8629-8633.
    • (1985) Prod. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 8629-8633
    • Podack, E.R.1    Young, J.D.E.2    Cohn, Z.A.3
  • 7
    • 0027479416 scopus 로고
    • Protease and Lymphocyte Cytotoxic Killing Mechanisms
    • Hudig, D.; Ewoldt, G. R.; Woodard, S. L. Protease and Lymphocyte Cytotoxic Killing Mechanisms. Curr. Opin. Immunol. 1993, 5, 90-96.
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 90-96
    • Hudig, D.1    Ewoldt, G.R.2    Woodard, S.L.3
  • 9
    • 0028952301 scopus 로고
    • Granzymes: Exogenous Proteinases that Induce Target Cell Apoptosis
    • Smyth, M. J.; Trapani, J. A. Granzymes: Exogenous Proteinases that Induce Target Cell Apoptosis. Immunol. Today 1995, 16, 202-206
    • (1995) Immunol. Today , vol.16 , pp. 202-206
    • Smyth, M.J.1    Trapani, J.A.2
  • 10
    • 0026474805 scopus 로고
    • Purification of Three Cytotoxic Lymphocyte Granule Serine Proteases that Induce Apoptosis through Distinct Substrate and Target Cell Interactions
    • Shi, L.; Kam, C.-M.; Powers, J. C.; Aebersold, R.; Greenberg, A. H. Purification of Three Cytotoxic Lymphocyte Granule Serine Proteases that Induce Apoptosis through Distinct Substrate and Target Cell Interactions. J. Exp. Med. 1992, 176, 1521-1529.
    • (1992) J. Exp. Med. , vol.176 , pp. 1521-1529
    • Shi, L.1    Kam, C.-M.2    Powers, J.C.3    Aebersold, R.4    Greenberg, A.H.5
  • 11
    • 0026532606 scopus 로고
    • A Natural Killer Cell Granule Protein that Induces DNA Fragmentation and Apoptosis
    • Shi, L.; Kraut, R. P.; Aebersold, R.; Greenberg, A. H. A Natural Killer Cell Granule Protein that Induces DNA Fragmentation and Apoptosis. J. Exp. Med. 1992, 175, 553-566.
    • (1992) J. Exp. Med. , vol.175 , pp. 553-566
    • Shi, L.1    Kraut, R.P.2    Aebersold, R.3    Greenberg, A.H.4
  • 12
    • 0026753388 scopus 로고
    • Cytotoxicity with Target DNA Breakdown by Rat Basophilic Leukemia Cells Expressing both Cytolysin and Granzyme A
    • Shiver, J. W.; Su, L.; Henkart, P. A. Cytotoxicity with Target DNA Breakdown by Rat Basophilic Leukemia Cells Expressing both Cytolysin and Granzyme A. Cell 1992, 71, 315-322.
    • (1992) Cell , vol.71 , pp. 315-322
    • Shiver, J.W.1    Su, L.2    Henkart, P.A.3
  • 13
    • 0028059276 scopus 로고
    • Granzyme A Released upon Stimulation of Cytotoxic T. Lymphocytes Activates the Thrombin Receptor on Neuronal Cells and Astrocytes
    • Suidan, H. S.; Bouvier, J.; Schaerer, E.; Stone, S. R.; Monard, D.; Tschopp, J. Granzyme A Released upon Stimulation of Cytotoxic T. Lymphocytes Activates the Thrombin Receptor on Neuronal Cells and Astrocytes. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 8112-8116.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 8112-8116
    • Suidan, H.S.1    Bouvier, J.2    Schaerer, E.3    Stone, S.R.4    Monard, D.5    Tschopp, J.6
  • 14
    • 0025805998 scopus 로고
    • Mouse T-cell Associated Serine Proteinase 1 Degrades Collagen Type IV: A Structural Basis for the Migration of Lymphocytes Through Vascular Basement Membranes
    • Simon, M. M.; Kramer, M. D.; Prester, M.; Gay, S. Mouse T-cell Associated Serine Proteinase 1 Degrades Collagen Type IV: A Structural Basis for the Migration of Lymphocytes Through Vascular Basement Membranes. Immunology 1991, 73, 117-119.
    • (1991) Immunology , vol.73 , pp. 117-119
    • Simon, M.M.1    Kramer, M.D.2    Prester, M.3    Gay, S.4
  • 15
    • 0023513615 scopus 로고
    • A Novel Serine Proteinase (HuTSP) Isolated from a Cloned Human CD8+ Cytolytic T Cell Line is Expressed and Secreted by Activated CD4+ and CD8+ Lymphocytes
    • Fruth, U.; Sinigaglia, F.; Schlesier, M.; Kilgus, J.; Kramer, M. D.; Simon, M. M. A Novel Serine Proteinase (HuTSP) Isolated from a Cloned Human CD8+ Cytolytic T Cell Line is Expressed and Secreted by Activated CD4+ and CD8+ Lymphocytes. Eur. J. Immunol. 1987, 17, 1625-1633.
    • (1987) Eur. J. Immunol. , vol.17 , pp. 1625-1633
    • Fruth, U.1    Sinigaglia, F.2    Schlesier, M.3    Kilgus, J.4    Kramer, M.D.5    Simon, M.M.6
  • 16
    • 0026078467 scopus 로고
    • The Enzymatic Activity of Human Cytotoxic T-Lymphocyte Granzyme A and Cytolysis Mediated by Cytotoxic T-Lymphocytes are Potently Inhibited by a Synthetic Antiprotease, FUT 175
    • Poe, M.; Wu, J. K.; Blake, J. T.; Zweerink, H. J.; Sigal, N. H. The Enzymatic Activity of Human Cytotoxic T-Lymphocyte Granzyme A and Cytolysis Mediated by Cytotoxic T-Lymphocytes are Potently Inhibited by a Synthetic Antiprotease, FUT 175. Arch. Biochem. Biophys. 1991, 284, 215-218.
    • (1991) Arch. Biochem. Biophys. , vol.284 , pp. 215-218
    • Poe, M.1    Wu, J.K.2    Blake, J.T.3    Zweerink, H.J.4    Sigal, N.H.5
  • 17
    • 0025962661 scopus 로고
    • Human Cytotoxic Lymphocyte Granzyme B: Its Purification from Granules and the Characterization of Substrate and Inhibitor Specificity
    • Poe, M.; Blake, J. T.; Boulton, D. A.; Gammon, M.; Sigal, N. H.; Wu, J. K.; Zweerink, H. J. Human Cytotoxic Lymphocyte Granzyme B: Its Purification from Granules and the Characterization of Substrate and Inhibitor Specificity. J. Biol. Chem. 1991, 266, 98-103.
    • (1991) J. Biol. Chem. , vol.266 , pp. 98-103
    • Poe, M.1    Blake, J.T.2    Boulton, D.A.3    Gammon, M.4    Sigal, N.H.5    Wu, J.K.6    Zweerink, H.J.7
  • 18
    • 0025212267 scopus 로고
    • Different Mouse Mast Cell Populations Express Various Combinations of at Least Six Distinct Mast Cell Serine Proteases
    • Reynolds, D. S.; Stevens, R. L.; Lane, W. S.; Carr, W. H.; Austen, K. F.; Serafin, W. E. Different Mouse Mast Cell Populations Express Various Combinations of at Least Six Distinct Mast Cell Serine Proteases. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 3230-3234.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3230-3234
    • Reynolds, D.S.1    Stevens, R.L.2    Lane, W.S.3    Carr, W.H.4    Austen, K.F.5    Serafin, W.E.6
  • 19
    • 0025971396 scopus 로고
    • Human and Murine Cytotoxic T Lymphocyte Serine Proteases: Subsite Mapping with Peptide Thioesters Substrates and Inhibition of Enzyme Activity and Cytolysis by Isocoumarins
    • Odake, S.; Kam, C.-H.; Narasimnah, L.; Poe, M.; Blake, J. T.; Krahenbuhl, O.; Tschopp, J.; Powers, J. C. Human and Murine Cytotoxic T Lymphocyte Serine Proteases: Subsite Mapping with Peptide Thioesters Substrates and Inhibition of Enzyme Activity and Cytolysis by Isocoumarins. Biochemistry 1991, 30, 2217-2227.
    • (1991) Biochemistry , vol.30 , pp. 2217-2227
    • Odake, S.1    Kam, C.-H.2    Narasimnah, L.3    Poe, M.4    Blake, J.T.5    Krahenbuhl, O.6    Tschopp, J.7    Powers, J.C.8
  • 20
    • 0024424969 scopus 로고
    • Selective Isocoumarin Serine Protease Inhibitors Block RNK-16 Lymphocyte Granule-Mediated Cytolysis
    • Hudig, D.; Allison, N. J.; Kam, C.-M.; Powers, J. C. Selective Isocoumarin Serine Protease Inhibitors Block RNK-16 Lymphocyte Granule-Mediated Cytolysis. Mol. Immunol. 1989, 26, 793-798.
    • (1989) Mol. Immunol. , vol.26 , pp. 793-798
    • Hudig, D.1    Allison, N.J.2    Kam, C.-M.3    Powers, J.C.4
  • 21
    • 5244277903 scopus 로고
    • Purification of Thrombin and Isolation of a Peptide Containing the Active Center Histidine
    • Glover, G.; Shaw, E. Purification of Thrombin and Isolation of a Peptide Containing the Active Center Histidine. J. Biol. Chem. 1971, 246, 4594-4601.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4594-4601
    • Glover, G.1    Shaw, E.2
  • 22
    • 0022550548 scopus 로고
    • p-Amidino Esters are Irreversible Inhibitors of Factor IXa and Xa and Thrombin
    • Turner, A. D.; Monroe, D. M.; Roberts, H. R.; Porter, N. A.; Pizzo, S. V. p-Amidino Esters are Irreversible Inhibitors of Factor IXa and Xa and Thrombin. Biochemistry 1986, 25, 4929-4935.
    • (1986) Biochemistry , vol.25 , pp. 4929-4935
    • Turner, A.D.1    Monroe, D.M.2    Roberts, H.R.3    Porter, N.A.4    Pizzo, S.V.5
  • 24
    • 0022396629 scopus 로고
    • Reaction of Serine Proteases with Substituted 3-Alkoxy-4-chloroisocoumarins and 3-Alkoxy-7amino-4-chloroisocoumarins. New Reactive Mechanism Based Inhibitors
    • Harper, J. W.; Powers, J. C. Reaction of Serine Proteases with Substituted 3-Alkoxy-4-chloroisocoumarins and 3-Alkoxy-7amino-4-chloroisocoumarins. New Reactive Mechanism Based Inhibitors. Biochemistry 1985, 24, 7200-7213.
    • (1985) Biochemistry , vol.24 , pp. 7200-7213
    • Harper, J.W.1    Powers, J.C.2
  • 25
    • 0022860034 scopus 로고
    • Inhibition of Chymotrypsin by Phosphonate and Phosphonamidate Peptide Analogues
    • Bartlett, P. A.; Lamden, L. A. Inhibition of Chymotrypsin by Phosphonate and Phosphonamidate Peptide Analogues. Bioorg. Chem. 1986, 14, 356-377.
    • (1986) Bioorg. Chem. , vol.14 , pp. 356-377
    • Bartlett, P.A.1    Lamden, L.A.2
  • 26
    • 0021106050 scopus 로고
    • Aminoalkylphosphonofluoridate Derivatives: Rapid and Potentially Selective Inactivators of Serine Peptidases
    • Lamden, L. A.; Bartlett, P. A. Aminoalkylphosphonofluoridate Derivatives: Rapid and Potentially Selective Inactivators of Serine Peptidases. Biochem. Biophys. Res. Commun. 1983, 112, 1085-1090.
    • (1983) Biochem. Biophys. Res. Commun. , vol.112 , pp. 1085-1090
    • Lamden, L.A.1    Bartlett, P.A.2
  • 27
    • 0024341633 scopus 로고
    • Irreversible Inhibition of Serine Proteases by Peptidyl Derivatives of a-Aminoalkylphosphonate Diphenyl Esters
    • Oleksyszyn, J.; Powers, J. C. Irreversible Inhibition of Serine Proteases by Peptidyl Derivatives of a-Aminoalkylphosphonate Diphenyl Esters. Biochem. Biophys. Res. Commun. 1989, 161, 143-149.
    • (1989) Biochem. Biophys. Res. Commun. , vol.161 , pp. 143-149
    • Oleksyszyn, J.1    Powers, J.C.2
  • 28
    • 0025979246 scopus 로고
    • Irreversible Inhibition of Serine Proteases by Peptide Derivatives of (α-Aminoalkyl)phosphonate Diphenyl Esters
    • Oleksyszyn, J.; Powers, J. C. Irreversible Inhibition of Serine Proteases by Peptide Derivatives of (α-Aminoalkyl)phosphonate Diphenyl Esters. Biochemistry 1991, 30, 485-493.
    • (1991) Biochemistry , vol.30 , pp. 485-493
    • Oleksyszyn, J.1    Powers, J.C.2
  • 29
    • 0028113356 scopus 로고
    • Chymase-Directed Serine Protease Inhibitor that Reacts with a Single 30-kDa Granzyme and Blocks NK-Mediated Cytotoxicity
    • Woodard, S. L.; Jackson, D. S.; Abuelyaman, A. S.; Powers, J. C.; Winkler, U.; Hudig, D. Chymase-Directed Serine Protease Inhibitor that Reacts with a Single 30-kDa Granzyme and Blocks NK-Mediated Cytotoxicity. J. Immunol. 1994, 153, 5016-5025.
    • (1994) J. Immunol. , vol.153 , pp. 5016-5025
    • Woodard, S.L.1    Jackson, D.S.2    Abuelyaman, A.S.3    Powers, J.C.4    Winkler, U.5    Hudig, D.6
  • 31
    • 0027230517 scopus 로고
    • A Convenient Synthesis of N-Protected Diphenyl Phosphonate Esters Analogues of Ornithine, Lysine, and Homolysine
    • Hamilton, R.; Walker, B. J.; Walker, B. A Convenient Synthesis of N-Protected Diphenyl Phosphonate Esters Analogues of Ornithine, Lysine, and Homolysine. Tetrahedron Lett. 1993, 34 2847-2850.
    • (1993) Tetrahedron Lett. , vol.34 , pp. 2847-2850
    • Hamilton, R.1    Walker, B.J.2    Walker, B.3
  • 33
    • 0028057482 scopus 로고
    • Novel Amidine-Containing Peptidyl Phosphonates as Irreversible Inhibitors for Blood Coagulation and Related Serine Proteaaes
    • Oleksyszyn, J.; Boduszek, B.; Kam, C.-M.; Powers, J. C. Novel Amidine-Containing Peptidyl Phosphonates as Irreversible Inhibitors for Blood Coagulation and Related Serine Proteaaes. J. Med. Chem. 1994, 37, 226-231.
    • (1994) J. Med. Chem. , vol.37 , pp. 226-231
    • Oleksyszyn, J.1    Boduszek, B.2    Kam, C.-M.3    Powers, J.C.4
  • 34
    • 0026021450 scopus 로고
    • Expression of the Protease Gene HF as a Marker in Rejecting Allogeneic Murine Heart Transplants
    • Mueller, C.; Shelby, J.; Weissman, I. L.; Perinat-Frey, T.; Eich wald, E. J. Expression of the Protease Gene HF as a Marker in Rejecting Allogeneic Murine Heart Transplants. Transplantation 1991, 57, 514-517.
    • (1991) Transplantation , vol.57 , pp. 514-517
    • Mueller, C.1    Shelby, J.2    Weissman, I.L.3    Perinat-Frey, T.4    Eich wald, E.J.5
  • 37
    • 12644312578 scopus 로고
    • Oxidation of Long-Chain and Related Alcohols to Carbonyls by Dimethyl Sulfoxide "Activated" by Oxalyl Chloride
    • Mancuso, A. J.; Huang, S.-L.; Swern, D. Oxidation of Long-Chain and Related Alcohols to Carbonyls by Dimethyl Sulfoxide "Activated" by Oxalyl Chloride. J. Org. Chem. 1978, 43, 2480-2482.
    • (1978) J. Org. Chem. , vol.43 , pp. 2480-2482
    • Mancuso, A.J.1    Huang, S.-L.2    Swern, D.3
  • 39
    • 0000736889 scopus 로고
    • An Improved Synthesis of Carbamates
    • Loev, B.; Kormendy, M. F. An Improved Synthesis of Carbamates. J. Org. Chem. 1963, 28, 3421-3426.
    • (1963) J. Org. Chem. , vol.28 , pp. 3421-3426
    • Loev, B.1    Kormendy, M.F.2
  • 40
    • 0029971695 scopus 로고    scopus 로고
    • Inhibition of Trypsin and Thrombin by Amino(4-amidinophenyl)methanephosphonate Diphenyl Ester Derivatives: X-ray Structures and Molecular Models
    • Bertrand, J. A.; Oleksyszyn, J.; Kam, C.-M.; Boduszek, B.; Presnell, S.; Plaskon, R. R.; Suddath, F. L.; Powers, J. C.; Williams, L. D. Inhibition of Trypsin and Thrombin by Amino(4-amidinophenyl)methanephosphonate Diphenyl Ester Derivatives: X-ray Structures and Molecular Models. Biochemistry 1996, 35, 3147-3155.
    • (1996) Biochemistry , vol.35 , pp. 3147-3155
    • Bertrand, J.A.1    Oleksyszyn, J.2    Kam, C.-M.3    Boduszek, B.4    Presnell, S.5    Plaskon, R.R.6    Suddath, F.L.7    Powers, J.C.8    Williams, L.D.9
  • 41
    • 0027070909 scopus 로고
    • Mast Cell Tryptases: Examination of Unusual Characteristics by Multiple Sequence Alignment and Molecular Modeling
    • Johnson, D. A.; Barton, G.J. Mast Cell Tryptases: Examination of Unusual Characteristics by Multiple Sequence Alignment and Molecular Modeling. Protein Sci. 1992, 1, 370-377.
    • (1992) Protein Sci. , vol.1 , pp. 370-377
    • Johnson, D.A.1    Barton, G.J.2
  • 44
    • 0011830309 scopus 로고
    • Cloning and Chromosomal Assignment of a Human cDNA Encoding a T Cell- And Natural Killer Cell-Specific Trypsin-Like Serine Protease
    • Gershenfeld, H. K.; Hershberger, R. J.; Shows, T. B.; Weissman, I. L. Cloning and Chromosomal Assignment of a Human cDNA Encoding a T Cell- and Natural Killer Cell-Specific Trypsin-Like Serine Protease. Proc. Natl. Acad. Sci. U.S.A. 1988, 85, 1184-1188.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 1184-1188
    • Gershenfeld, H.K.1    Hershberger, R.J.2    Shows, T.B.3    Weissman, I.L.4
  • 45
    • 0024434198 scopus 로고
    • Cloning and Characterization of Complementary DNA for Human Tryptase
    • Miller, J. S.; Westin, E. H.; Schwartz, L. B. Cloning and Characterization of Complementary DNA for Human Tryptase. J. Clin. Invest. 1989, 84, 1188-1195.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1188-1195
    • Miller, J.S.1    Westin, E.H.2    Schwartz, L.B.3
  • 46
    • 0016291686 scopus 로고
    • Structure of the Complex formed by Bovine Trypsin and Bovine Pancreatic Trypsin Inhibitor. II. Crystallographic refinement at 1.9 A Resolution
    • Huber, R.; KuKla, D.; Bode, W.; Schwager, P.; Bartels, K.; Diesenhofer, J.; Steigemann, W. Structure of the Complex formed by Bovine Trypsin and Bovine Pancreatic Trypsin Inhibitor. II. Crystallographic refinement at 1.9 A Resolution. J. Mol. Biol. 1974, 89, 73-101.
    • (1974) J. Mol. Biol. , vol.89 , pp. 73-101
    • Huber, R.1    Kukla, D.2    Bode, W.3    Schwager, P.4    Bartels, K.5    Diesenhofer, J.6    Steigemann, W.7
  • 48
    • 0029166828 scopus 로고
    • Active Site-Directed Thrombin Inhibitors: α-Hydroxyacyl-Prolyl-Arginals. New Orally Active Stable Analogues of D-Phe-Pro-Arg-H
    • Bajusz, S.; Barabás, E.; Fauszt, I.; Fehér, A.; Horvtáh, G.; Juhász, A.; Szabó, A. G.; Széll, E. Active Site-Directed Thrombin Inhibitors: α-Hydroxyacyl-Prolyl-Arginals. New Orally Active Stable Analogues of D-Phe-Pro-Arg-H. Bioorg. Med. Chem. 1995, 3, 1079-1089.
    • (1995) Bioorg. Med. Chem. , vol.3 , pp. 1079-1089
    • Bajusz, S.1    Barabás, E.2    Fauszt, I.3    Fehér, A.4    Horvtáh, G.5    Juhász, A.6    Szabó, A.G.7    Széll, E.8
  • 51
    • 0021684932 scopus 로고
    • Kinetics of Hydrolysis of Peptide Thioester Derivatives of Arginine by Human and Bovine Thrombin
    • Cook, R. R.; McRae, B. J.; Powers, J. C. Kinetics of Hydrolysis of Peptide Thioester Derivatives of Arginine by Human and Bovine Thrombin. Arch. Biochem. Biophys. 1984, 234, 82-88.
    • (1984) Arch. Biochem. Biophys. , vol.234 , pp. 82-88
    • Cook, R.R.1    McRae, B.J.2    Powers, J.C.3
  • 53
    • 0021336801 scopus 로고
    • Natural Killer Activity in the Rat. III. Characterization of Transplan table Large Lymphocyte (LGL) Leukemias in the F344 Rat
    • Reynolds, C. W.; Bere, J. E. W.; Ward, J. M. Natural Killer Activity in the Rat. III. Characterization of Transplan table Large Lymphocyte (LGL) Leukemias in the F344 Rat. J. Immunol. 1984, 132, 534-540.
    • (1984) J. Immunol. , vol.132 , pp. 534-540
    • Reynolds, C.W.1    Bere, J.E.W.2    Ward, J.M.3
  • 54
    • 0028903558 scopus 로고
    • Human Mast Cell Tryptase Isoforms: Separation and Examination of Substrate-Specificity Differences
    • Little, S.; Johnson, D. A. Human Mast Cell Tryptase Isoforms: Separation and Examination of Substrate-Specificity Differences. Biochem. J. 1995, 307, 341-346.
    • (1995) Biochem. J. , vol.307 , pp. 341-346
    • Little, S.1    Johnson, D.A.2
  • 55
    • 0021148042 scopus 로고
    • Human Lung Tryptase. Purification and Characterization
    • Smith, T. J.; Houghland, M. W.; Johnson, D. A. Human Lung Tryptase. Purification and Characterization. J. Biol. Chem. 1984, 259, 11046-11051.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11046-11051
    • Smith, T.J.1    Houghland, M.W.2    Johnson, D.A.3
  • 56
    • 0019888627 scopus 로고
    • Tryptase from Human Pulmonary Mast Cells. Purification and Characterization
    • Schwartz, L. B.; Lewis, R. A.; Austen, K. F. Tryptase from Human Pulmonary Mast Cells. Purification and Characterization. J. Biol. Chem. 1981, 256, 11939-11943.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11939-11943
    • Schwartz, L.B.1    Lewis, R.A.2    Austen, K.F.3
  • 57
    • 0015546107 scopus 로고
    • Determination of the Operational Molarity of Solutions of Bovine α-Chymotrypsin, Trypsin, Thrombin, and Factor Xa by Spectrofluorometric Titration
    • Jameson, G. W.; Roberts, D. V.; Adams, R. W.; Kyle, W. S. A.; Elmore, D. T. Determination of the Operational Molarity of Solutions of Bovine α-Chymotrypsin, Trypsin, Thrombin, and Factor Xa by Spectrofluorometric Titration. Biochem. J. 1973, 131, 107-117.
    • (1973) Biochem. J. , vol.131 , pp. 107-117
    • Jameson, G.W.1    Roberts, D.V.2    Adams, R.W.3    Kyle, W.S.A.4    Elmore, D.T.5
  • 58
    • 0019254107 scopus 로고
    • Colorimetric Method for the Assay of Heparin Content in Immobilized Heparin Preparations
    • Smith, P. K.; Mallia, A. K.; Hermanson, G. T. Colorimetric Method for the Assay of Heparin Content in Immobilized Heparin Preparations. Anal. Biochem. 1980, 109, 466-473.
    • (1980) Anal. Biochem. , vol.109 , pp. 466-473
    • Smith, P.K.1    Mallia, A.K.2    Hermanson, G.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.