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Volumn 42, Issue 20, 1999, Pages 4161-4171

6-Substituted 2-oxo-2H-1-benzopyran-3-carboxylic acid as a core structure for specific inhibitors of human leukocyte elastase

Author keywords

[No Author keywords available]

Indexed keywords

5 CHLOROPYRID 3 YL 6 ACETOXYMETHYL 2 OXO 2H 1 BENZOPYRAN 3 CARBOXYLIC ACID; 6 CHLOROPYRID 2 YL 6 CHLOROMETHYL 2 OXO 2H 1 BENZOPYRAN 3 CARBOXYLIC ACID; CHYMOTRYPSIN A; ENZYME INHIBITOR; LEUKOCYTE ELASTASE; THROMBIN; UNCLASSIFIED DRUG;

EID: 0033533761     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm990070k     Document Type: Article
Times cited : (68)

References (41)
  • 1
    • 0028282060 scopus 로고
    • Synthetic inhibitors of elastase
    • Edwards, P. D.; Bernstein, P. R. Synthetic inhibitors of elastase. Med. Res. Rev. 1994, 14, 127-194.
    • (1994) Med. Res. Rev. , vol.14 , pp. 127-194
    • Edwards, P.D.1    Bernstein, P.R.2
  • 2
    • 0002943240 scopus 로고
    • Synthetic substrates and inhibitors of thrombin
    • Berliner, L. J., Eds.; Plenum Press: New York, London
    • Powers, J. C.; Kam, C. M. Synthetic substrates and inhibitors of thrombin. In Thrombin, Structure and Function; Berliner, L. J., Eds.; Plenum Press: New York, London, 1992; pp 117-158.
    • (1992) Thrombin, Structure and Function , pp. 117-158
    • Powers, J.C.1    Kam, C.M.2
  • 3
    • 0022746525 scopus 로고
    • Inhibition of serine proteases by peptidyl fluoromethyl ketones
    • Imperiali, B.; Abeles, R. H. Inhibition of serine proteases by peptidyl fluoromethyl ketones. Biochemistry 1986, 25, 3760-3767.
    • (1986) Biochemistry , vol.25 , pp. 3760-3767
    • Imperiali, B.1    Abeles, R.H.2
  • 4
    • 0022856832 scopus 로고
    • The synthesis of peptidylfluoromethanes and their properties as inhibitors of serine proteinases and cysteine proteinases
    • Rauber, P.; Angliker, H.; Walker, B.; Shaw, E. The synthesis of peptidylfluoromethanes and their properties as inhibitors of serine proteinases and cysteine proteinases. Biochem. J. 1986, 239, 633-640.
    • (1986) Biochem. J. , vol.239 , pp. 633-640
    • Rauber, P.1    Angliker, H.2    Walker, B.3    Shaw, E.4
  • 5
    • 0023098752 scopus 로고
    • The synthesis of lysylfluoromethanes and their properties as inhibitors of trypsin, plasmin and cathepsin B
    • (a) Angliker, H.; Wikstrom, P.; Rauber, P.; Shaw, E. The synthesis of lysylfluoromethanes and their properties as inhibitors of trypsin, plasmin and cathepsin B. Biochem. J. 1987, 241, 871-875.
    • (1987) Biochem. J. , vol.241 , pp. 871-875
    • Angliker, H.1    Wikstrom, P.2    Rauber, P.3    Shaw, E.4
  • 6
    • 0021723091 scopus 로고
    • Inhibition of the serine proteases leukocyte elastase, pancreatic elastase, cathepsin G, and chymotrypsin by peptide boronic acids
    • (b) Kettner, C. A.; Shenvi, A. B. Inhibition of the serine proteases leukocyte elastase, pancreatic elastase, cathepsin G, and chymotrypsin by peptide boronic acids. J. Biol. Chem. 1984, 259, 15106-15114.
    • (1984) J. Biol. Chem. , vol.259 , pp. 15106-15114
    • Kettner, C.A.1    Shenvi, A.B.2
  • 7
    • 0032548152 scopus 로고    scopus 로고
    • Design and synthesis of hydrazinopeptides and their evaluation as human leukocyte elastase inhibitors
    • Guy, L.; Vidal, J.; Collet, A.; Amour, A.; Reboud-Ravaux, M. Design and synthesis of hydrazinopeptides and their evaluation as human leukocyte elastase inhibitors. J. Med. Chem. 1998, 41, 4833-4843.
    • (1998) J. Med. Chem. , vol.41 , pp. 4833-4843
    • Guy, L.1    Vidal, J.2    Collet, A.3    Amour, A.4    Reboud-Ravaux, M.5
  • 8
    • 0022356416 scopus 로고
    • Acylamino boronic acids and difluoroborane analogues of amino acids: Potent inhibitors of chymotrypsin and elastase
    • Kinder, D. H.; Katzenellenbogen, J. A. Acylamino boronic acids and difluoroborane analogues of amino acids: potent inhibitors of chymotrypsin and elastase. J. Med. Chem. 1985, 28, 1917-1925.
    • (1985) J. Med. Chem. , vol.28 , pp. 1917-1925
    • Kinder, D.H.1    Katzenellenbogen, J.A.2
  • 9
    • 0023463943 scopus 로고
    • Complex of alpha-chymotrypsin and N-acetyl-L-leucyl-L-phenylalanyl trifluoromethyl ketone: Structural studies with NMR spectroscopy
    • Liang, T. C.; Abeles, R. H. Complex of alpha-chymotrypsin and N-acetyl-L-leucyl-L-phenylalanyl trifluoromethyl ketone: structural studies with NMR spectroscopy. Biochemistry 1987, 26, 7603-7608.
    • (1987) Biochemistry , vol.26 , pp. 7603-7608
    • Liang, T.C.1    Abeles, R.H.2
  • 10
    • 0025098316 scopus 로고
    • Design and synthesis of 4H-3,1-benzoxazin-4-ones as potent alternate substrate inhibitors of human leukocyte elastase
    • Krantz, A.; Spencer, R. W.; Tam, T. F.; Liak, T. J.; Copp, L. J.; Thomas, E. M.; Rafferty, S. P. Design and synthesis of 4H-3,1-benzoxazin-4-ones as potent alternate substrate inhibitors of human leukocyte elastase. J. Med. Chem. 1990, 33, 464-479.
    • (1990) J. Med. Chem. , vol.33 , pp. 464-479
    • Krantz, A.1    Spencer, R.W.2    Tam, T.F.3    Liak, T.J.4    Copp, L.J.5    Thomas, E.M.6    Rafferty, S.P.7
  • 11
    • 0027428786 scopus 로고
    • 5-Methyl-4H-3,1-benzoxazin-4-one derivatives: Specific inhibitors of human leukocyte elastase
    • Uejima, Y.; Kokubo, M.; Oshida, J.; Kawabata, H.; Kato, Y.; Fujii, K. 5-Methyl-4H-3,1-benzoxazin-4-one derivatives: specific inhibitors of human leukocyte elastase. J. Pharmacol. Exp. Ther. 1993, 265, 516-523.
    • (1993) J. Pharmacol. Exp. Ther. , vol.265 , pp. 516-523
    • Uejima, Y.1    Kokubo, M.2    Oshida, J.3    Kawabata, H.4    Kato, Y.5    Fujii, K.6
  • 12
    • 0026445446 scopus 로고
    • Enol lactone derivatives as inhibitors of human neutrophil elastase and trypsin-like proteases
    • Katzenellenbogen, J. A.; Rai, R.; Dai, W. Enol lactone derivatives as inhibitors of human neutrophil elastase and trypsin-like proteases. Bioorg. Med. Chem. Lett. 1992, 2, 1399-1404.
    • (1992) Bioorg. Med. Chem. Lett. , vol.2 , pp. 1399-1404
    • Katzenellenbogen, J.A.1    Rai, R.2    Dai, W.3
  • 13
    • 0026499282 scopus 로고
    • Guanidinophenyl-substituted enol lactones as selective, mechanism-based inhibitors of trypsinlike serine proteases
    • Rai, R.; Katzenellenbogen, J. A. Guanidinophenyl-substituted enol lactones as selective, mechanism-based inhibitors of trypsinlike serine proteases. J. Med. Chem. 1992, 35, 4150-4159.
    • (1992) J. Med. Chem. , vol.35 , pp. 4150-4159
    • Rai, R.1    Katzenellenbogen, J.A.2
  • 14
    • 0029072042 scopus 로고
    • Mechanism-based isocoumarin inhibitors for human leukocyte elastase. Effect of the 7-amino substituent and 3-alkoxy group in 3-alkoxy-7-amino-4-chloroisocoumarins on inhibitory potency
    • Kerrigan, J. E.; Oleksyszyn, J.; Kam, C. M.; Selzler, J.; Powers, J. C. Mechanism-based isocoumarin inhibitors for human leukocyte elastase. Effect of the 7-amino substituent and 3-alkoxy group in 3-alkoxy-7-amino-4-chloroisocoumarins on inhibitory potency. J. Med. Chem. 1995, 38, 544-5452.
    • (1995) J. Med. Chem. , vol.38 , pp. 544-5452
    • Kerrigan, J.E.1    Oleksyszyn, J.2    Kam, C.M.3    Selzler, J.4    Powers, J.C.5
  • 16
    • 0028921957 scopus 로고
    • Phosphonates and phosphinates: Novel leaving groups for benzisothiazolone inhibitors of human leukocyte elastase
    • Desai, R. C.; Court, J. C.; Ferguson, E.; Gordon, R. J.; Hlasta, D. J.; Dunlap, R. P.; Franke, C. A. Phosphonates and phosphinates: novel leaving groups for benzisothiazolone inhibitors of human leukocyte elastase. J. Med. Chem. 1995, 38, 1571-1574.
    • (1995) J. Med. Chem. , vol.38 , pp. 1571-1574
    • Desai, R.C.1    Court, J.C.2    Ferguson, E.3    Gordon, R.J.4    Hlasta, D.J.5    Dunlap, R.P.6    Franke, C.A.7
  • 22
    • 0030175241 scopus 로고    scopus 로고
    • Interaction of human leukocyte elastase with a N-aryl azetidinone suicide substrate: Conformational analyses based on the mechanism of action of serine proteinases
    • Vergely, I.; Laugaa, P.; Reboud-Ravaux, M. Interaction of human leukocyte elastase with a N-aryl azetidinone suicide substrate: Conformational analyses based on the mechanism of action of serine proteinases. J. Mol. Graph. 1996, 14, 158-167, 145.
    • (1996) J. Mol. Graph. , vol.14 , pp. 158-167
    • Vergely, I.1    Laugaa, P.2    Reboud-Ravaux, M.3
  • 28
    • 0027715472 scopus 로고
    • Inhibition of human leukocyte elastase. 5. Inhibition by 6-alkyl substituted penem benzyl esters
    • Finke, P. E.; Dahlgren, M. E.; Weston, H.; Maycock, A. L.; Doherty, J. B. Inhibition of human leukocyte elastase. 5. Inhibition by 6-alkyl substituted penem benzyl esters. Bioorg. Med. Chem. Lett. 1993, 3, 2277-2282.
    • (1993) Bioorg. Med. Chem. Lett. , vol.3 , pp. 2277-2282
    • Finke, P.E.1    Dahlgren, M.E.2    Weston, H.3    Maycock, A.L.4    Doherty, J.B.5
  • 29
    • 0030993410 scopus 로고    scopus 로고
    • Structure-based design of a general class of mechanism-based inhibitors of the serine proteinases employing a novel amino acid-derived heterocyclic scaffold
    • Groutas, W. C.; Kuang, R.; Venkataraman, R.; Epp, J. B.; Ruan, S.; Prakash, O. Structure-based design of a general class of mechanism-based inhibitors of the serine proteinases employing a novel amino acid-derived heterocyclic scaffold. Biochemistry 1997, 36, 4739-4750.
    • (1997) Biochemistry , vol.36 , pp. 4739-4750
    • Groutas, W.C.1    Kuang, R.2    Venkataraman, R.3    Epp, J.B.4    Ruan, S.5    Prakash, O.6
  • 30
    • 0030014368 scopus 로고    scopus 로고
    • Esters and amides of 6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylic acid as inhibitors of alpha-chymotrypsin: Significance of the "aromatic" nature of the novel ester-type coumarin for strong inhibitory activity
    • Pochet, L.; Doucet, C.; Schynts, M.; Thierry, N.; Boggetto, N.; Pirotte, B.; Jiang, K. Y.; Masereel, B.; de Tullio, P.; Delarge, J.; Reboud-Ravaux, M. Esters and amides of 6-(chloromethyl)-2-oxo-2H-1-benzopyran-3-carboxylic acid as inhibitors of alpha-chymotrypsin: significance of the "aromatic" nature of the novel ester-type coumarin for strong inhibitory activity. J. Med. Chem. 1996, 39, 2579-2585.
    • (1996) J. Med. Chem. , vol.39 , pp. 2579-2585
    • Pochet, L.1    Doucet, C.2    Schynts, M.3    Thierry, N.4    Boggetto, N.5    Pirotte, B.6    Jiang, K.Y.7    Masereel, B.8    De Tullio, P.9    Delarge, J.10    Reboud-Ravaux, M.11
  • 32
    • 0015861774 scopus 로고
    • i) and the concentration of inhibitor which causes 50% inhibition (IC50) of an enzymatic reaction
    • i) and the concentration of inhibitor which causes 50% inhibition (IC50) of an enzymatic reaction. Biochem. Pharmacol. 1973, 22, 3099-3108.
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 34
    • 0021745792 scopus 로고
    • Inactivation of human high-and low-molecular-weight urokinases. Analysis of their active site
    • Reboud-Ravaux, M.; Desvages, G. Inactivation of human high-and low-molecular-weight urokinases. Analysis of their active site. Biochim. Biophys. Acta 1984, 791, 333-341.
    • (1984) Biochim. Biophys. Acta , vol.791 , pp. 333-341
    • Reboud-Ravaux, M.1    Desvages, G.2
  • 35
    • 0017399918 scopus 로고
    • Inactivation of alpha-chymotrypsin by new bifunctional reagents: Halomethylated derivatives of dihydrocoumarins
    • Béchet, J. J.; Dupaix, A.; Blagoeva, I. Inactivation of alpha-chymotrypsin by new bifunctional reagents: halomethylated derivatives of dihydrocoumarins. Biochimie 1977, 59, 231-239.
    • (1977) Biochimie , vol.59 , pp. 231-239
    • Béchet, J.J.1    Dupaix, A.2    Blagoeva, I.3
  • 36
    • 0017326665 scopus 로고
    • Reaction of serine proteases with aza-amino acid and aza-peptide derivatives
    • Powers, J. C.; Gupton, B. F. Reaction of serine proteases with aza-amino acid and aza-peptide derivatives. Methods Enzymol. 1977, 46, 208-216.
    • (1977) Methods Enzymol. , vol.46 , pp. 208-216
    • Powers, J.C.1    Gupton, B.F.2
  • 38
    • 77956987594 scopus 로고
    • Titration of trypsin, plasmin, and thrombin with p-nitrophenyl p′-guanidinobenzoate HCl
    • Chase, T. J.; Shaw, E. Titration of trypsin, plasmin, and thrombin with p-nitrophenyl p′-guanidinobenzoate HCl. Methods Enzymol. 1970, 19, 20-27.
    • (1970) Methods Enzymol. , vol.19 , pp. 20-27
    • Chase, T.J.1    Shaw, E.2
  • 39
    • 0027270445 scopus 로고
    • New mechanism-based inactivators of trypsin-like proteinases. Selective inactivation of urokinase by functionalized cyclopeptides incorporating a sulfoniomethyl-substituted m-aminobenzoic acid residue
    • Wakselman, M.; Xie, J.; Mazaleyrat, J. P.; Boggetto, N.; Vilain, A. C.; Montagne, J. J.; Reboud-Ravaux, M. New mechanism-based inactivators of trypsin-like proteinases. Selective inactivation of urokinase by functionalized cyclopeptides incorporating a sulfoniomethyl-substituted m-aminobenzoic acid residue. J. Med. Chem. 1993, 36, 1539-1547.
    • (1993) J. Med. Chem. , vol.36 , pp. 1539-1547
    • Wakselman, M.1    Xie, J.2    Mazaleyrat, J.P.3    Boggetto, N.4    Vilain, A.C.5    Montagne, J.J.6    Reboud-Ravaux, M.7
  • 40
    • 73649151319 scopus 로고
    • Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
    • Kitz, R.; Wilson, I. B. Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase. J. Biol. Chem. 1962, 237, 3245-3249.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3245-3249
    • Kitz, R.1    Wilson, I.B.2


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