메뉴 건너뛰기




Volumn 69, Issue 3, 2007, Pages 170-179

Synthesis of peptidyl ene diones: Selective inactivators of the cysteine proteinases

Author keywords

Cysteine proteinase inactivators; Ene diones

Indexed keywords

2 1 (BENZYL 4 ETHOXYCARBONYL 2 OXO BUT 3 ENYLCARBAMOYL)PYRROLIDINE 1 CARBOXYLIC ACID BENZYLESTER; 5 5 (N BENZYLOXYCARBONYLAMINO) 4 OXO 6 PHENYLETHYLHEX 2 ENOATE; 5 5 (N BENZYLOXYCARBONYLAMINO) 6 METHYL 4 OXO 2 ETHYLHEPTENOATE; 5 METHYL 5 [2' 2' (BENZYLOXYCARBONYLAMINO) 3' PHENYLPROPANOYLAMINO] 4 OXO HEX 2 ENAL; CATHEPSIN B; CATHEPSIN L; CATHEPSIN S; CHYMOTRYPSIN; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; ESTER; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

EID: 34247269043     PISSN: 17470277     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2007.00490.x     Document Type: Article
Times cited : (4)

References (33)
  • 6
    • 0021260942 scopus 로고
    • Vinylogous amino-acid esters - a new class of inactivators for thiol proteases
    • Hanzlik R.P., Thompson S.A. (1984) Vinylogous amino-acid esters - a new class of inactivators for thiol proteases. J Med Chem;27:711-712.
    • (1984) J Med Chem , vol.27 , pp. 711-712
    • Hanzlik, R.P.1    Thompson, S.A.2
  • 7
    • 0026517333 scopus 로고
    • Structure-activity relationships for the inhibition of papain by peptide Michael acceptors
    • Liu S., Hanzlik R.P. (1992) Structure-activity relationships for the inhibition of papain by peptide Michael acceptors. J Med Chem;35:1067-1075.
    • (1992) J Med Chem , vol.35 , pp. 1067-1075
    • Liu, S.1    Hanzlik, R.P.2
  • 10
    • 0029099619 scopus 로고
    • Vinyl sulfones as mechanism-based cysteine protease inhibitors
    • Palmer J.T., Rasnick D., Klaus J.L., Bromme D. (1995) Vinyl sulfones as mechanism-based cysteine protease inhibitors. J Med Chem;38:3193-3196.
    • (1995) J Med Chem , vol.38 , pp. 3193-3196
    • Palmer, J.T.1    Rasnick, D.2    Klaus, J.L.3    Bromme, D.4
  • 11
    • 0029911570 scopus 로고    scopus 로고
    • Peptidyl vinyl sulphones: A new class of potent and selective cysteine protease inhibitors
    • Bromme D., Klaus J.L., Okamoto K., Rasnick D., Palmer J.T. (1996) Peptidyl vinyl sulphones: a new class of potent and selective cysteine protease inhibitors. Biochem J;315:85-89.
    • (1996) Biochem J , vol.315 , pp. 85-89
    • Bromme, D.1    Klaus, J.L.2    Okamoto, K.3    Rasnick, D.4    Palmer, J.T.5
  • 13
    • 0033030776 scopus 로고    scopus 로고
    • Localization of rat cathepsin K in osteoclasts and resorption pits: Inhibition of bone resorption and cathepsin K-activity by peptidyl vinyl sulfones
    • Xia L.H., Kilb J., Wex H., Li Z.Q., Lipyansky A., Breuil V., Stein L., Palmer J.T., Dempster D.W., Bromme D. (1999) Localization of rat cathepsin K in osteoclasts and resorption pits: inhibition of bone resorption and cathepsin K-activity by peptidyl vinyl sulfones. Biol Chem;380:679-687.
    • (1999) Biol Chem , vol.380 , pp. 679-687
    • Xia, L.H.1    Kilb, J.2    Wex, H.3    Li, Z.Q.4    Lipyansky, A.5    Breuil, V.6    Stein, L.7    Palmer, J.T.8    Dempster, D.W.9    Bromme, D.10
  • 14
    • 0015606478 scopus 로고
    • Human cathepsin-B - purification and some properties of the enzyme
    • Barrett A.J. (1973) Human cathepsin-B - purification and some properties of the enzyme. Biochem J;131:809-822.
    • (1973) Biochem J , vol.131 , pp. 809-822
    • Barrett, A.J.1
  • 15
    • 0025884209 scopus 로고
    • High-performance liquid-chromatographic method for the simultaneous purification of cathepsin-B, cathepsin-H and cathepsin-L from human liver
    • Dalet-Fumeron V., Guinec N., Pagano M. (1991) High-performance liquid-chromatographic method for the simultaneous purification of cathepsin-B, cathepsin-H and cathepsin-L from human liver. J Chromatogr Biomed Appl;568:55-68.
    • (1991) J Chromatogr Biomed Appl , vol.568 , pp. 55-68
    • Dalet-Fumeron, V.1    Guinec, N.2    Pagano, M.3
  • 16
    • 0029996205 scopus 로고    scopus 로고
    • High level expression and crystallization of recombinant human cathepsin S
    • Bromme D., McGrath M.E. (1996) High level expression and crystallization of recombinant human cathepsin S. Protein Sci;5:789-791.
    • (1996) Protein Sci , vol.5 , pp. 789-791
    • Bromme, D.1    McGrath, M.E.2
  • 17
    • 0018341904 scopus 로고
    • Rapid procedure for the large-scale purification of elastase and cathepsin-G from human sputum
    • Martodam R.R., Baugh R.J., Twumasi D.Y., Lieher I.E. (1979) Rapid procedure for the large-scale purification of elastase and cathepsin-G from human sputum. Prep Biochem;9:15-31.
    • (1979) Prep Biochem , vol.9 , pp. 15-31
    • Martodam, R.R.1    Baugh, R.J.2    Twumasi, D.Y.3    Lieher, I.E.4
  • 18
    • 0019887728 scopus 로고
    • Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases
    • Green G.D.J., Shaw E. (1981) Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases. J Biol Chem;256:1923-1928.
    • (1981) J Biol Chem , vol.256 , pp. 1923-1928
    • Green, G.D.J.1    Shaw, E.2
  • 19
    • 37049085854 scopus 로고
    • Oxidation of alpha-diazoketones derived from L-amino acids and dipeptides using dimethyldioxirane - synthesis and reactions of homochiral N-protected alpha-amino glyoxals
    • Darkins P., McCarthy N., McKervey M.A., Tao Y. (1993) Oxidation of alpha-diazoketones derived from L-amino acids and dipeptides using dimethyldioxirane - synthesis and reactions of homochiral N-protected alpha-amino glyoxals. J Chem Soc, Chem Commun;15:1222-1223.
    • (1993) J Chem Soc, Chem Commun , vol.15 , pp. 1222-1223
    • Darkins, P.1    McCarthy, N.2    McKervey, M.A.3    Tao, Y.4
  • 20
    • 0015546107 scopus 로고
    • Determination of operational molarity of solutions of bovine alpha-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. (1973) Determination of operational molarity of solutions of bovine alpha-chymotrypsin, trypsin, thrombin and factor Xa by spectrofluorometric titration. Biochem J;131:101-117.
    • (1973) Biochem J , vol.131 , pp. 101-117
    • Jameson, G.W.1    Roberts, D.V.2    Adams, R.W.3    Kyle, W.S.A.4    Elmore, D.T.5
  • 21
    • 0019765848 scopus 로고
    • Cathepsin-B, cathepsin-H, and cathepsin-L
    • Barrett A.J., Kirschke H. (1981) Cathepsin-B, cathepsin-H, and cathepsin-L. Methods Enzymol;80:535-561.
    • (1981) Methods Enzymol , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 22
    • 0003744057 scopus 로고
    • Cambridge: Cambridge University Press;p
    • Roberts D.V. (1977) Enzyme Kinetics. Cambridge: Cambridge University Press;p. 299-306.
    • (1977) Enzyme Kinetics , pp. 299-306
    • Roberts, D.V.1
  • 23
    • 0014211618 scopus 로고    scopus 로고
    • Schecter I., Berger A. (1967) On the size of the active site in proteases: I. Papain. Biochem Biophys Res Commun;27:157-162.
    • Schecter I., Berger A. (1967) On the size of the active site in proteases: I. Papain. Biochem Biophys Res Commun;27:157-162.
  • 24
    • 0020473244 scopus 로고
    • Determination of the rate-constant of enzyme modification by measuring the substrate reaction in the presence of modifier
    • Tian W.-X., Tsou C.-L. (1982) Determination of the rate-constant of enzyme modification by measuring the substrate reaction in the presence of modifier. Biochemistry;21:1028-1032.
    • (1982) Biochemistry , vol.21 , pp. 1028-1032
    • Tian, W.-X.1    Tsou, C.-L.2
  • 25
    • 0021234203 scopus 로고
    • The irreversible inhibition of urokinase, kidney-cell plasminogen-activator, plasmin and beta-trypsin by 1-(n-6-amino-n-hexyl)carbamoylimidazole
    • Walker B., Elmore D.T. (1984) The irreversible inhibition of urokinase, kidney-cell plasminogen-activator, plasmin and beta-trypsin by 1-(n-6-amino-n-hexyl)carbamoylimidazole. Biochem J;221:277-280.
    • (1984) Biochem J , vol.221 , pp. 277-280
    • Walker, B.1    Elmore, D.T.2
  • 26
  • 27
    • 0025908898 scopus 로고
    • Peptidyl (acyloxy)methyl ketones and the quiescent affinity label concept - the departing group as a variable structural element in the design of inactivators of cysteine proteinases
    • Krantz A., Copp L.J., Coles P.J., Smith R.A., Hearb S.B. (1991) Peptidyl (acyloxy)methyl ketones and the quiescent affinity label concept - the departing group as a variable structural element in the design of inactivators of cysteine proteinases. Biochemistry;30:4678-4687.
    • (1991) Biochemistry , vol.30 , pp. 4678-4687
    • Krantz, A.1    Copp, L.J.2    Coles, P.J.3    Smith, R.A.4    Hearb, S.B.5
  • 28
    • 0022607084 scopus 로고
    • Carboxyl-modified amino-acids and peptides as protease inhibitors
    • Thompson S.A., Andrews P.R., Hanzlik R.P. (1985) Carboxyl-modified amino-acids and peptides as protease inhibitors. J Med Chem;29:104-111.
    • (1985) J Med Chem , vol.29 , pp. 104-111
    • Thompson, S.A.1    Andrews, P.R.2    Hanzlik, R.P.3
  • 29
    • 0016700753 scopus 로고
    • Tight-binding inhibitors: 1. Kinetic-behaviour
    • Cha S. (1975) Tight-binding inhibitors: 1. Kinetic-behaviour. Biochem Pharmacol;24:2177-2185.
    • (1975) Biochem Pharmacol , vol.24 , pp. 2177-2185
    • Cha, S.1
  • 30
    • 0001396685 scopus 로고
    • The slow-binding and slow, tight-binding inhibition of enzyme-catalyzed reactions
    • Morrison J.F. (1982) The slow-binding and slow, tight-binding inhibition of enzyme-catalyzed reactions. Trends Biochem Sci;7:102-105.
    • (1982) Trends Biochem Sci , vol.7 , pp. 102-105
    • Morrison, J.F.1
  • 31
    • 0019891335 scopus 로고
    • Rapid inactivation of cathepsin-l by Z-Phe-PheCHN2-1 and Z-Phe-AlaCHN2
    • Kirschke H., Shaw E. (1981) Rapid inactivation of cathepsin-l by Z-Phe-PheCHN2-1 and Z-Phe-AlaCHN2. Biochem Biophys Res Commun;101:454-458.
    • (1981) Biochem Biophys Res Commun , vol.101 , pp. 454-458
    • Kirschke, H.1    Shaw, E.2
  • 32
    • 0021103783 scopus 로고
    • An exploration of the primary specificity site of cathepsin-B
    • Shaw E., Wikstrom P., Ruscica J. (1983) An exploration of the primary specificity site of cathepsin-B. Arch Biochem Biophys;222:424-429.
    • (1983) Arch Biochem Biophys , vol.222 , pp. 424-429
    • Shaw, E.1    Wikstrom, P.2    Ruscica, J.3
  • 33
    • 0023855444 scopus 로고
    • Active-center differences between cathepsin-L and cathepsin-B - the S1 binding region
    • Kirschke H., Wikstrom P., Shaw E. (1988) Active-center differences between cathepsin-L and cathepsin-B - the S1 binding region. FEBS Lett, 228:128-130.
    • (1988) FEBS Lett , vol.228 , pp. 128-130
    • Kirschke, H.1    Wikstrom, P.2    Shaw, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.