메뉴 건너뛰기




Volumn 42, Issue 4, 1999, Pages 560-572

New peptidic cysteine protease inhibitors derived from the electrophilic α-amino acid aziridine-2,3-dicarboxylic acid

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMINO ACID; AZIRIDINE 2,3 DICARBOXYLIC ACID; CYSTEINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 0033602268     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm981061z     Document Type: Article
Times cited : (64)

References (78)
  • 1
    • 0343433408 scopus 로고    scopus 로고
    • Cysteine proteases and their inhibitors
    • Schirmeister, T.; Otto, H.-H. Cysteine proteases and their inhibitors. Chem. Rev. 1997, 97, 133-171.
    • (1997) Chem. Rev. , vol.97 , pp. 133-171
    • Schirmeister, T.1    Otto, H.-H.2
  • 2
    • 30244571682 scopus 로고
    • The structure of papain
    • Boyer, P. D., Ed.; Academic Press: New York
    • Drenth, J.; Jansonius, J. N.; Koekoeck, R.; Wolters, B. G. The structure of papain. In The Enzymes; Boyer, P. D., Ed.; Academic Press: New York, 1971; Vol. 3, pp 485-499.
    • (1971) The Enzymes , vol.3 , pp. 485-499
    • Drenth, J.1    Jansonius, J.N.2    Koekoeck, R.3    Wolters, B.G.4
  • 3
    • 0024208917 scopus 로고
    • A malarial cysteine proteinase is necessary for hemoglobin degradation by plasmodium falciparum
    • Rosenthal, P.; McKerrow, J.; Aikawa, M.; Nagasawa, H.; Leech, J. A malarial cysteine proteinase is necessary for hemoglobin degradation by Plasmodium falciparum. J. Clin. Invest. 1988, 82, 1560-1566.
    • (1988) J. Clin. Invest. , vol.82 , pp. 1560-1566
    • Rosenthal, P.1    McKerrow, J.2    Aikawa, M.3    Nagasawa, H.4    Leech, J.5
  • 4
    • 0028673327 scopus 로고
    • Families of cysteine peptidases
    • Rawlings, N. D.; Barrett, A. J. Families of cysteine peptidases. Methods Enzymol. 1994, 244, 461-486.
    • (1994) Methods Enzymol. , vol.244 , pp. 461-486
    • Rawlings, N.D.1    Barrett, A.J.2
  • 5
  • 6
    • 0025086765 scopus 로고
    • Activities of calcium-activated neutral proteases and its endogenous inhibitor in skeletal muscle of dystrophic hamster
    • Kawashima, S.; Nakamura, M.; Hayashi, M. Activities of calcium-activated neutral proteases and its endogenous inhibitor in skeletal muscle of dystrophic hamster. Biol. Chem. Hoppe-Seyler 1990, 371 (Suppl.), 205-210.
    • (1990) Biol. Chem. Hoppe-seyler , vol.371 , Issue.SUPPL. , pp. 205-210
    • Kawashima, S.1    Nakamura, M.2    Hayashi, M.3
  • 8
    • 0029240263 scopus 로고
    • Mammalian cysteine protease inhibitors: Biochemical properties and possible roles in tumor progression
    • Calkins, C.; Sloane, B. Mammalian cysteine protease inhibitors: Biochemical properties and possible roles in tumor progression. Biol. Chem. Hoppe-Seyler 1995, 376, 71-80.
    • (1995) Biol. Chem. Hoppe-Seyler , vol.376 , pp. 71-80
    • Calkins, C.1    Sloane, B.2
  • 9
    • 0020571105 scopus 로고
    • Role of cellular proteinases in acute myocardial infarction. I. Proteolysis in nonischemic and ischemic rat myocardium and the effects of antipain, leupeptin, pepstatin, and chymostatin administered in vivo
    • Bolli, R.; Cannon, R.; Speir, E.; Goldstein, R.; Epstein, S. Role of cellular proteinases in acute myocardial infarction. I. Proteolysis in nonischemic and ischemic rat myocardium and the effects of antipain, leupeptin, pepstatin, and chymostatin administered in vivo. J. Am. Coll. Cardiol. 1983, 2, 681-688.
    • (1983) J. Am. Coll. Cardiol. , vol.2 , pp. 681-688
    • Bolli, R.1    Cannon, R.2    Speir, E.3    Goldstein, R.4    Epstein, S.5
  • 10
    • 0019887728 scopus 로고
    • Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases
    • Green, G.; Shaw, E. Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases. J. Biol. Chem. 1981, 256, 1923-1928.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1923-1928
    • Green, G.1    Shaw, E.2
  • 11
    • 0026602248 scopus 로고
    • Inactivation of calpain by peptidyl fluoromethyl ketones
    • Angliker, H.; Anagli, J.; Shaw, E. Inactivation of calpain by peptidyl fluoromethyl ketones. J. Med. Chem. 1992, 35, 216-220.
    • (1992) J. Med. Chem. , vol.35 , pp. 216-220
    • Angliker, H.1    Anagli, J.2    Shaw, E.3
  • 12
    • 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.; Coles, P.; Smith, R.; Heard, S. 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 1991, 30, 4678-4687.
    • (1991) Biochemistry , vol.30 , pp. 4678-4687
    • Krantz, A.1    Copp, L.2    Coles, P.3    Smith, R.4    Heard, S.5
  • 14
    • 0029099619 scopus 로고
    • Vinyl sulfones as mechanism-based cysteine protease inhibitors
    • Palmer, J.; Rasnick, D.; Klaus, J.; Brömme, D. Vinyl sulfones as mechanism-based cysteine protease inhibitors. J. Med. Chem. 1995, 38, 3193-3196.
    • (1995) J. Med. Chem. , vol.38 , pp. 3193-3196
    • Palmer, J.1    Rasnick, D.2    Klaus, J.3    Brömme, D.4
  • 15
    • 0008287081 scopus 로고
    • Drugs Future 1994, 19, 1039-1040.
    • (1994) Drugs Future , vol.19 , pp. 1039-1040
  • 16
    • 0023950936 scopus 로고
    • 13C NMR characterization of the site of alkylation
    • 13C NMR characterization of the site of alkylation. J. Am. Chem. Soc. 1988, 110, 4043-4044.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 4043-4044
    • Yabe, Y.1    Guillaume, D.2    Rich, D.3
  • 18
    • 0019486009 scopus 로고
    • Effects on cathepsins B, H and D in pectoral muscle of dystrophic chickens (line 413) of in vivo administration of E-64-c (N-[N-(L-3-transcarboxyoxirane-2-carbonyl)-L-leucyl]-3-methylbutylamine)
    • (a) Noda, T.; Isogal, K.; Katunuma, N.; Tarumoto, Y.; Ohzeki, M. Effects on cathepsins B, H and D in pectoral muscle of dystrophic chickens (line 413) of in vivo administration of E-64-c (N-[N-(L-3-transcarboxyoxirane-2-carbonyl)-L-leucyl]-3-methylbutylamine). J. Biochem. 1981, 90, 893-896.
    • (1981) J. Biochem. , vol.90 , pp. 893-896
    • Noda, T.1    Isogal, K.2    Katunuma, N.3    Tarumoto, Y.4    Ohzeki, M.5
  • 19
    • 0023037165 scopus 로고
    • (b) Drugs Future 1986, 11, 927-930.
    • (1986) Drugs Future , vol.11 , pp. 927-930
  • 20
    • 0022997931 scopus 로고
    • In vitro and in vivo inhibition of cysteine proteinases by EST, a new analogue of E-64
    • Tamai, M.; Matsumoto, K.; Ohmura, S.; Koyama, I.; Ozawa, Y.; Hanada, K. In vitro and in vivo inhibition of cysteine proteinases by EST, a new analogue of E-64. J. Pharmacobio-Dyn. 1986, 9, 672-677.
    • (1986) J. Pharmacobio-Dyn. , vol.9 , pp. 672-677
    • Tamai, M.1    Matsumoto, K.2    Ohmura, S.3    Koyama, I.4    Ozawa, Y.5    Hanada, K.6
  • 23
    • 0019948262 scopus 로고
    • L-trans-epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    • Barrett, A.; Kembhavi, A.; Brown, M.; Kirschke, H.; Knight, C.; Tamai, M.; Hanada, K. L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem. J. 1982, 201, 189-198.
    • (1982) Biochem. J. , vol.201 , pp. 189-198
    • Barrett, A.1    Kembhavi, A.2    Brown, M.3    Kirschke, H.4    Knight, C.5    Tamai, M.6    Hanada, K.7
  • 26
    • 0028908350 scopus 로고
    • Crystal structure of cathepsin B inhibited with CA030 at 2.0-angstrom resolution: A basis for the design of specific epoxysuccinyl inhibitors
    • Turk, D.; Podobnik, M.; Popovic, T.; Katunuma, N.; Bode, W.; Huber, R.; Turk, V. Crystal structure of cathepsin B inhibited with CA030 at 2.0-Angstrom resolution: A basis for the design of specific epoxysuccinyl inhibitors. Biochemistry 1995, 34, 4791-4794.
    • (1995) Biochemistry , vol.34 , pp. 4791-4794
    • Turk, D.1    Podobnik, M.2    Popovic, T.3    Katunuma, N.4    Bode, W.5    Huber, R.6    Turk, V.7
  • 27
    • 0023640271 scopus 로고
    • Reaction of aziridine-carboxylic acids with thiols in aqueous solution. The formation of β-amino acids
    • Hata, Y.; Watanabe, M. Reaction of aziridine-carboxylic acids with thiols in aqueous solution. The formation of β-amino acids. Tetrahedron 1987, 43, 3881-3888.
    • (1987) Tetrahedron , vol.43 , pp. 3881-3888
    • Hata, Y.1    Watanabe, M.2
  • 28
    • 0029130176 scopus 로고
    • Aziridine analogues of [[trans-(epoxysuccinyl)-L-leucyl]amino]-4-guanidinobutane (E-64) as inhibitors of cysteine proteases
    • Martichonok, V.; Plouffe, C.; Storer, A.; Ménard, R.; Jones, J. B. Aziridine analogues of [[trans-(epoxysuccinyl)-L-leucyl]amino]-4-guanidinobutane (E-64) as inhibitors of cysteine proteases. J. Med. Chem. 1995, 38, 3078-3085.
    • (1995) J. Med. Chem. , vol.38 , pp. 3078-3085
    • Martichonok, V.1    Plouffe, C.2    Storer, A.3    Ménard, R.4    Jones, J.B.5
  • 32
    • 0029948116 scopus 로고    scopus 로고
    • Aziridine-2,3-dicarboxylic acid derivatives as inhibitors of papain
    • Schirmeister, T. Aziridine-2,3-dicarboxylic acid derivatives as inhibitors of papain. Arch. Pharm. Pharm. Med. Chem. 1997, 329, 239-244.
    • (1997) Arch. Pharm. Pharm. Med. Chem. , vol.329 , pp. 239-244
    • Schirmeister, T.1
  • 33
    • 0025726305 scopus 로고
    • Synthesis of naturally occurring(2s,3S)-(+)-aziridine-2,3-dicarboxylic acid
    • Legters, J.; Thijs, L.; Zwanenburg, B. Synthesis of naturally occurring(2S,3S)-(+)-aziridine-2,3-dicarboxylic acid. Tetrahedron 1991, 47, 5287-5294.
    • (1991) Tetrahedron , vol.47 , pp. 5287-5294
    • Legters, J.1    Thijs, L.2    Zwanenburg, B.3
  • 34
    • 0003130388 scopus 로고
    • Stereoselective synthesis of optically active forms of δ-multistriatin, the attractant for european populations of the smaller european elm bark beetle
    • Mori, K.; Iwasawa, H. Stereoselective synthesis of optically active forms of δ-multistriatin, the attractant for european populations of the smaller european elm bark beetle. Tetrahedron 1980, 36, 87-90.
    • (1980) Tetrahedron , vol.36 , pp. 87-90
    • Mori, K.1    Iwasawa, H.2
  • 35
    • 0001337335 scopus 로고
    • Stereochemical course of 5-lipoxygenation of arachidonate by rat basophil leukemic cell (RBL-1) and potato enzymes
    • Corey, E.; Lansbury, P., Jr. Stereochemical course of 5-lipoxygenation of arachidonate by rat basophil leukemic cell (RBL-1) and potato enzymes. J. Am. Chem. Soc. 1983, 105, 4093-4094.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 4093-4094
    • Corey, E.1    Lansbury P., Jr.2
  • 37
    • 0014412486 scopus 로고
    • A new convenient reagent for peptide synthesis
    • Belleau, B.; Malek, G. A new convenient reagent for peptide synthesis. J. Am. Chem. Soc. 1968, 90, 1651-1652.
    • (1968) J. Am. Chem. Soc. , vol.90 , pp. 1651-1652
    • Belleau, B.1    Malek, G.2
  • 39
    • 0002203126 scopus 로고
    • Chiral synthons by ester hydrolysis catalyzed by pig liver esterase
    • Ohno, M.; Otsuka, M. Chiral synthons by ester hydrolysis catalyzed by Pig Liver Esterase. Org. React. 1989, 37, 1-55.
    • (1989) Org. React. , vol.37 , pp. 1-55
    • Ohno, M.1    Otsuka, M.2
  • 40
    • 0345384641 scopus 로고    scopus 로고
    • note
    • 4 and evaporated in vacuo. Without enzymes no hydrolysis of 17a took place.
  • 41
    • 0028167180 scopus 로고
    • P1 aspartate-based peptide α-((2,6-dichlorobenzyl)-oxy)methyl ketones as potent time-dependent inhibitors of interleukin-1β-converting enzyme
    • Dolle, R.; Hoyer, D.; Prasad, C.; Schmidt, S.; Helaszek, C.; Miller, R.; Ator, M. P1 Aspartate-based peptide α-((2,6-dichlorobenzyl)-oxy)methyl ketones as potent time-dependent inhibitors of Interleukin-1β-Converting Enzyme. J. Med. Chem. 1994, 37, 563-564.
    • (1994) J. Med. Chem. , vol.37 , pp. 563-564
    • Dolle, R.1    Hoyer, D.2    Prasad, C.3    Schmidt, S.4    Helaszek, C.5    Miller, R.6    Ator, M.7
  • 42
    • 0029744988 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of papain by epoxysuccinyl inhibitors
    • Meara, J. P.; Rich, D. H. Mechanistic studies on the inactivation of papain by epoxysuccinyl inhibitors. J. Med. Chem. 1996, 39, 3357-3366.
    • (1996) J. Med. Chem. , vol.39 , pp. 3357-3366
    • Meara, J.P.1    Rich, D.H.2
  • 44
    • 0022182469 scopus 로고
    • Calpain inhibition by peptide epoxides
    • Parkes, C.; Kembhavi, A.; Barrett, A. Calpain inhibition by peptide epoxides. Biochem. J. 1985, 230, 509-516.
    • (1985) Biochem. J. , vol.230 , pp. 509-516
    • Parkes, C.1    Kembhavi, A.2    Barrett, A.3
  • 45
    • 0027371777 scopus 로고
    • Stereoselective hydrolysis of dimethyl aziridin-2,3-dicarboxylates with pig liver esterase (PLE)
    • Renold, P.; Tamm, C. Stereoselective hydrolysis of dimethyl aziridin-2,3-dicarboxylates with pig liver esterase (PLE). Tetrahedron Asymmetry 1993, 4, 2295-2298.
    • (1993) Tetrahedron Asymmetry , vol.4 , pp. 2295-2298
    • Renold, P.1    Tamm, C.2
  • 46
    • 0027215523 scopus 로고
    • Candida cylindracea lipase-catalyzed hydrolysis of methyl aziridine-2-carboxylates and -2,3-dicarboxylates
    • Bucciarelli, M.; Forni, A.; Moretti, I.; Prati, F.; Torre, G. Candida cylindracea lipase-catalyzed hydrolysis of methyl aziridine-2-carboxylates and -2,3-dicarboxylates. Tetrahedron Asymmetry 1993, 4, 903-906.
    • (1993) Tetrahedron Asymmetry , vol.4 , pp. 903-906
    • Bucciarelli, M.1    Forni, A.2    Moretti, I.3    Prati, F.4    Torre, G.5
  • 47
    • 0014936053 scopus 로고
    • Studies on the Bacillus subtilis neutral-protease- and bacillus thermoproteolyticus thermolysin-catalyzed hydrolysis of dipeptide substrates
    • Feder, J.; Schuck, J. M. Studies on the Bacillus subtilis Neutral-Protease- and Bacillus thermoproteolyticus Thermolysin-catalyzed hydrolysis of dipeptide substrates. Biochemistry 1970, 9, 2784-2791.
    • (1970) Biochemistry , vol.9 , pp. 2784-2791
    • Feder, J.1    Schuck, J.M.2
  • 49
    • 0017138215 scopus 로고
    • Binding of chloromethyl ketone substrate analogues to crystalline papain
    • Drenth, J.; Kalk, H.; Swen, H. Binding of chloromethyl ketone substrate analogues to crystalline papain. Biochemistry 1976, 15, 3731-3738.
    • (1976) Biochemistry , vol.15 , pp. 3731-3738
    • Drenth, J.1    Kalk, H.2    Swen, H.3
  • 50
    • 0029984218 scopus 로고    scopus 로고
    • Peptidyl epoxides: Novel selevtive inactivators of cysteine proteases
    • Albeck, A.; Fluss, S.; Persky, R. Peptidyl epoxides: Novel selevtive inactivators of cysteine proteases. J. Am. Chem. Soc. 1996, 118, 3591-3596.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3591-3596
    • Albeck, A.1    Fluss, S.2    Persky, R.3
  • 51
    • 0013632679 scopus 로고
    • Azomethinylide
    • Klamann, D., Hagemann, H., Eds.; Thieme: Stuttgart
    • Claus, P. Azomethinylide. In Methoden Org. Chem. (Houben-Weyl); Klamann, D., Hagemann, H., Eds.; Thieme: Stuttgart, 1990; Vol. E14b, Part 1, pp 88-91.
    • (1990) Methoden Org. Chem. (Houben-weyl) , vol.E14B , Issue.1 PART , pp. 88-91
    • Claus, P.1
  • 54
    • 0015937127 scopus 로고
    • Kinetics of papain-catalyzed hydrolysis of α-N-benzoyl-L-arginine-p-nitroanilide
    • Mole, J. E.; Horton, H. R. Kinetics of papain-catalyzed hydrolysis of α-N-benzoyl-L-arginine-p-nitroanilide. Biochemistry 1973, 12, 816-822.
    • (1973) Biochemistry , vol.12 , pp. 816-822
    • Mole, J.E.1    Horton, H.R.2
  • 56
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L
    • Barrett, A.; Kirschke, H. Cathepsin B, cathepsin H, and cathepsin L. Methods Enzymol. 1981, 80, 535-561.
    • (1981) Methods Enzymol. , vol.80 , pp. 535-561
    • Barrett, A.1    Kirschke, H.2
  • 57
    • 0029882882 scopus 로고    scopus 로고
    • Cathepsin L is an intracellular and extracellular protease in Paramecium tetraurelia. Purification, cloning, sequencing and specific inhibition by its expressed propeptide
    • Völkel, H.; Kurz, U.; Linder, J.; Klumpp, S.; Gnau, V.; Jung, G.; Schultz, J. Cathepsin L is an intracellular and extracellular protease in Paramecium tetraurelia. Purification, cloning, sequencing and specific inhibition by its expressed propeptide. Eur. J. Biochem. 1996, 238, 198-206.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 198-206
    • Völkel, H.1    Kurz, U.2    Linder, J.3    Klumpp, S.4    Gnau, V.5    Jung, G.6    Schultz, J.7
  • 58
    • 0027977957 scopus 로고
    • E-64 analogues as inhibitors of cathepsin L and cathepsin S: Importance of the S2-P2 interactions for potency and selectivity
    • Gour-Salin, B.; Lachance, P.; Bonneau, P.; Storer, A.; Kirschke, H.; Broemme, D. E-64 Analogues as inhibitors of cathepsin L and cathepsin S: Importance of the S2-P2 interactions for potency and selectivity. Bioorg. Chem. 1994, 22, 227-241.
    • (1994) Bioorg. Chem. , vol.22 , pp. 227-241
    • Gour-Salin, B.1    Lachance, P.2    Bonneau, P.3    Storer, A.4    Kirschke, H.5    Broemme, D.6
  • 59
    • 0021683468 scopus 로고
    • Comparative specificity and kinetic stucies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates
    • Sasaki, T.; Kikuchi, T.; Yumoto, N.; Yoshimura, N.; Murachi, T. Comparative specificity and kinetic stucies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates. J. Biol. Chem. 1984, 259, 12489-12494.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12489-12494
    • Sasaki, T.1    Kikuchi, T.2    Yumoto, N.3    Yoshimura, N.4    Murachi, T.5
  • 60
    • 0015947848 scopus 로고
    • Mechanism of reaction of human plasmin with α-N-benzoyl-L-arginine-p-nitroanilide (titration of the enzyme)
    • Christensen, U.; Muellertz, S. Mechanism of reaction of human plasmin with α-N-Benzoyl-L-arginine-p-nitroanilide (Titration of the enzyme). Biochim. Biophys. Acta 1974, 334, 187-190.
    • (1974) Biochim. Biophys. Acta , vol.334 , pp. 187-190
    • Christensen, U.1    Muellertz, S.2
  • 63
    • 0014431088 scopus 로고
    • A spectrophotometric assay for neutral protease
    • Feder, J. A spectrophotometric assay for neutral protease. Biochem. Biophys. Res. Commun. 1968, 32, 326-332.
    • (1968) Biochem. Biophys. Res. Commun. , vol.32 , pp. 326-332
    • Feder, J.1
  • 64
    • 0013793247 scopus 로고
    • Kinetics of the pepsin-catalyzed hydrolysis of N-acetyl-L-phenylalanyl-L-diiodotyrosine
    • Jackson, W.; Schlamowitz, M.; Shaw, A. Kinetics of the pepsin-catalyzed hydrolysis of N-acetyl-L-phenylalanyl-L-diiodotyrosine. Biochemistry 1965, 4, 1537-1543.
    • (1965) Biochemistry , vol.4 , pp. 1537-1543
    • Jackson, W.1    Schlamowitz, M.2    Shaw, A.3
  • 65
    • 0020473244 scopus 로고
    • Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier
    • Tian, W.-X.; Tsou, C.-L. Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier. Biochemistry 1982, 21, 1028-1032.
    • (1982) Biochemistry , vol.21 , pp. 1028-1032
    • Tian, W.-X.1    Tsou, C.-L.2
  • 66
    • 73649151319 scopus 로고
    • Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
    • Kitz, R.; Wilson, I. 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.2
  • 68
    • 0344058268 scopus 로고    scopus 로고
    • GraFit, version 3.0; Erithacus Software Ltd.: London, 1992
    • GraFit, version 3.0; Erithacus Software Ltd.: London, 1992.
  • 69
    • 0001095726 scopus 로고    scopus 로고
    • Addition of azoles and amines to unsymmetrical fumaric esters
    • Zaderenko, P.; López, M. C.; Ballesteros, P. Addition of azoles and amines to unsymmetrical fumaric esters. J. Org. Chem. 1996, 61, 6825-6828.
    • (1996) J. Org. Chem. , vol.61 , pp. 6825-6828
    • Zaderenko, P.1    López, M.C.2    Ballesteros, P.3
  • 70
    • 85066051603 scopus 로고
    • The michael type addition of free sulfilimine
    • Furukawa, N.; Oae, S. The Michael type addition of free sulfilimine. Synthesis 1976, 1, 30-32.
    • (1976) Synthesis , vol.1 , pp. 30-32
    • Furukawa, N.1    Oae, S.2
  • 71
    • 0344920582 scopus 로고    scopus 로고
    • note
    • 4) C,H,N. Assignment of NMR signals was carried out by INEPT long-range NMR spectroscopy. (matrix presented)
  • 72
    • 0344920581 scopus 로고    scopus 로고
    • note
    • -1).
  • 73
    • 0344058266 scopus 로고    scopus 로고
    • note
    • -1).
  • 74
    • 0344489471 scopus 로고    scopus 로고
    • note
    • -1.
  • 75
    • 0025364110 scopus 로고
    • Recent developments in inhibiting cysteine and serine proteases
    • Demuth, H. Recent developments in inhibiting cysteine and serine proteases. J. Enzyme Inhib. 1990, 3, 249-278.
    • (1990) J. Enzyme Inhib. , vol.3 , pp. 249-278
    • Demuth, H.1
  • 76
    • 33847800887 scopus 로고
    • The hard soft acids bases (HSAB) principle and organic chemistry
    • Ho, T.-L. The hard soft acids bases (HSAB) principle and organic chemistry. Chem. Rev. 1975, 75, 1-20.
    • (1975) Chem. Rev. , vol.75 , pp. 1-20
    • Ho, T.-L.1
  • 77
    • 0345351876 scopus 로고    scopus 로고
    • note
    • -1. The superposition has been performed using the program Multifit from Sybyl 6.4.
  • 78
    • 0344058263 scopus 로고    scopus 로고
    • note
    • The docking of 26a into the active site of papain has been performed using the program FlexiDock from the Sybyl 6.4 Biopolymer Module (Tripos Associates Inc., St. Louis, MO). Energy minimization: Tripos force field, Gasteiger-Hueckel charges on ligand, Kollmann charges on protein. As FlexiDock pocket a region of 0.4 nm around the amino acids Cys25, Tyr67, Pro68, Trp69, Val133, Val157, His159, Ala160, and Phe207 of papain has been defined. The structure of papain has been taken from the Brookhaven Protein Databank (entry 1pe6).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.