메뉴 건너뛰기




Volumn 33, Issue 3, 1996, Pages 135-162

Fluorogenic substrates for proteases based on intramolecular fluorescence energy transfer (IFETS)

Author keywords

Fluorescence; Intramolecular fluorescence energy transfer substrate; Intramolecular quenched fluorescent substrate; Protease

Indexed keywords

PROTEINASE;

EID: 0030607684     PISSN: 0165022X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-022X(96)00023-1     Document Type: Short Survey
Times cited : (73)

References (77)
  • 1
    • 0019752371 scopus 로고
    • Assay of coagulation proteases using peptide chromogenic substrates
    • [1] Lottenberg, R., Christensen, U., Jackson, C.M. and Coleman, P.L., Assay of coagulation proteases using peptide chromogenic substrates. Methods Enzymol., 80 (1981) 341-361.
    • (1981) Methods Enzymol. , vol.80 , pp. 341-361
    • Lottenberg, R.1    Christensen, U.2    Jackson, C.M.3    Coleman, P.L.4
  • 3
    • 0024118989 scopus 로고
    • Chromogenic and fluorogenic substrates for assay of proteolytic enzymes
    • [3] Gershkovich. A.A. and Kibirev, V.K., Chromogenic and fluorogenic substrates for assay of proteolytic enzymes. Bioorg. Khim., 14 (1988) 1461-1488.
    • (1988) Bioorg. Khim. , vol.14 , pp. 1461-1488
    • Gershkovich, A.A.1    Kibirev, V.K.2
  • 5
    • 0004240280 scopus 로고
    • W.A. Benjamin, New York, NY, 1965, 'Mir'. Moscow
    • [5] Turro, N.J.. Molecular Photochemistry, W.A. Benjamin, New York, NY, 1965, 'Mir'. Moscow, 1967, pp. 111-164.
    • (1967) Molecular Photochemistry , pp. 111-164
    • Turro, N.J.1
  • 7
    • 0018388950 scopus 로고
    • Intramolecularly quenched fluorogenic substrates for hydrolytic enzymes
    • [7] Yaron, A., Carmel, A. and Katchalski-Katzir, E., Intramolecularly quenched fluorogenic substrates for hydrolytic enzymes. Anal. Biochem., 95 (1979) 228-235.
    • (1979) Anal. Biochem. , vol.95 , pp. 228-235
    • Yaron, A.1    Carmel, A.2    Katchalski-Katzir, E.3
  • 8
    • 0028254178 scopus 로고
    • Fluorescent substrates of proteolytic enzymes with internal quenching of fluorescence
    • [8] Gershkovich, A.A.. Fluorescent substrates of proteolytic enzymes with internal quenching of fluorescence. Ukr. Biochem. J., 66 (1994) 10-42.
    • (1994) Ukr. Biochem. J. , vol.66 , pp. 10-42
    • Gershkovich, A.A.1
  • 10
    • 0011364625 scopus 로고
    • Distance distribution rescovered from steady-state fluorescence measurements on thirteen donor-acceptor pairs with different Förster distances
    • [10] Wiczk, W., Eis, P.S., Fishman, M.N.. Johnson, M.L. and Lakowicz, J.R., Distance distribution rescovered from steady-state fluorescence measurements on thirteen donor-acceptor pairs with different Förster distances. J. Fluorescence. 1 (1991) 273-286.
    • (1991) J. Fluorescence , vol.1 , pp. 273-286
    • Wiczk, W.1    Eis, P.S.2    Fishman, M.N.3    Johnson, M.L.4    Lakowicz, J.R.5
  • 11
  • 12
    • 0017577685 scopus 로고
    • Intramolecularly quenched fluorescent peptides as fluorogenic substrates of leucine aminopeptidase and inhibitors of clostrodial aminopeptidase
    • [12] Carmel, A., Kessler, E. and Yaron, A.. Intramolecularly quenched fluorescent peptides as fluorogenic substrates of leucine aminopeptidase and inhibitors of clostrodial aminopeptidase. Eur. J. Biochem., 73 (1977) 617-625.
    • (1977) Eur. J. Biochem. , vol.73 , pp. 617-625
    • Carmel, A.1    Kessler, E.2    Yaron, A.3
  • 14
    • 0025967144 scopus 로고
    • Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins
    • [14] Chagas, J.R., Juliano, L. and Prado, E.S., Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins. Anal. Biochem.. 192 (1991) 419-425.
    • (1991) Anal. Biochem.. , vol.192 , pp. 419-425
    • Chagas, J.R.1    Juliano, L.2    Prado, E.S.3
  • 15
    • 0025770925 scopus 로고
    • Antranilamide and nitrityrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidase: Multicolumn peptide synthesis of enzyme substrates for subtilysin Carlsberg and pepsin
    • [15] Meldal, M. and Breddam, K., Antranilamide and nitrityrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidase: multicolumn peptide synthesis of enzyme substrates for subtilysin Carlsberg and pepsin. Anal. Biochem., 195 (1991) 141-147.
    • (1991) Anal. Biochem. , vol.195 , pp. 141-147
    • Meldal, M.1    Breddam, K.2
  • 16
    • 0020586841 scopus 로고
    • Reactivity of bovine blood coagulation factor IX, factor X, and factor XI toward fluorogenic peptides containing the activation site sequences of bovine factor IX and factor X
    • [16] Castillo, M.J., Kurachi, K., Nishino, N., Ohkubo, I. and Powers, J.C., Reactivity of bovine blood coagulation factor IX, factor X, and factor XI toward fluorogenic peptides containing the activation site sequences of bovine factor IX and factor X. Biochemistry, 22 (1983) 1021-1029.
    • (1983) Biochemistry , vol.22 , pp. 1021-1029
    • Castillo, M.J.1    Kurachi, K.2    Nishino, N.3    Ohkubo, I.4    Powers, J.C.5
  • 17
    • 0017884203 scopus 로고
    • An intramolecularly quenched fluorescent tripeptide as a fluorogenic substrates of angiotensin-1-converting enzyme and of bacterial dipeptidyl carboxypeptidase
    • [17] Carmel, A. and Yaron, A., An intramolecularly quenched fluorescent tripeptide as a fluorogenic substrates of angiotensin-1-converting enzyme and of bacterial dipeptidyl carboxypeptidase. Eur. J. Biochem., 87 (1978) 265-273.
    • (1978) Eur. J. Biochem. , vol.87 , pp. 265-273
    • Carmel, A.1    Yaron, A.2
  • 18
    • 0021264335 scopus 로고
    • Fluoregenic substrates for the enkephalin-degrading neutral endopeptidase (enkephalinase)
    • [18] Rush, R.S., Motas, M., Powers, J.C., Tanaka, T. and Hersh, L.B., Fluoregenic substrates for the enkephalin-degrading neutral endopeptidase (enkephalinase). Arch. Biochem. Biophys., 231 (1984) 390-393.
    • (1984) Arch. Biochem. Biophys. , vol.231 , pp. 390-393
    • Rush, R.S.1    Motas, M.2    Powers, J.C.3    Tanaka, T.4    Hersh, L.B.5
  • 19
    • 0021802394 scopus 로고
    • Clostrodium histolyticum collagenase: Development of new thio ester, fluorogenic, and depsipeptide substrates and new inhibitors
    • [19] Vencill, C.F., Rasnick, D., Crumbley, K.V., Nishino, N. and Powers, J.C., Clostrodium histolyticum collagenase: development of new thio ester, fluorogenic, and depsipeptide substrates and new inhibitors. Biochemistry, 24 (1985) 3149-3157.
    • (1985) Biochemistry , vol.24 , pp. 3149-3157
    • Vencill, C.F.1    Rasnick, D.2    Crumbley, K.V.3    Nishino, N.4    Powers, J.C.5
  • 20
    • 0018963538 scopus 로고
    • Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand
    • [20] Nishino, N. and Powers, J.C., Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand. J. Biol. Chem., 255 (1980) 3482-3486.
    • (1980) J. Biol. Chem. , vol.255 , pp. 3482-3486
    • Nishino, N.1    Powers, J.C.2
  • 21
    • 0023319866 scopus 로고
    • N-Antraniloylation converts peptide p-nitroanilides into fluorogenic substrates of proteases without loss of their chromogenic properties
    • [21] Bratanova, E.K. and Petkov, D.D., N-Antraniloylation converts peptide p-nitroanilides into fluorogenic substrates of proteases without loss of their chromogenic properties. Anal. Biochem., 162 (1987) 213-218.
    • (1987) Anal. Biochem. , vol.162 , pp. 213-218
    • Bratanova, E.K.1    Petkov, D.D.2
  • 22
    • 0026716442 scopus 로고
    • N-Antraniloyl-Ala-Ala-Phe-4-nitroanilide, a highly sensitive substrate for subtilisins
    • [22] Stambolieva, N.A., Ivanov, I.P. and Yomtova, V.M., N-Antraniloyl-Ala-Ala-Phe-4-nitroanilide, a highly sensitive substrate for subtilisins. Arch. Biochem. Biophys., 294 (1992) 703-706.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 703-706
    • Stambolieva, N.A.1    Ivanov, I.P.2    Yomtova, V.M.3
  • 23
    • 0026503259 scopus 로고
    • Substrate preferences of glutamic acid specific endopeptidases assessed by synthetic peptide substrates which are based on the principle of intramolecular quenching
    • [23] Breddam, K. and Meldal, M., Substrate preferences of glutamic acid specific endopeptidases assessed by synthetic peptide substrates which are based on the principle of intramolecular quenching. Eur. J. Biochem., 206 (1992) 103-107.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 103-107
    • Breddam, K.1    Meldal, M.2
  • 24
    • 0026638586 scopus 로고
    • Extensive comparision of the substrate preferences of two subtilisins as determined with peptide substrates which are based on the principle of intramolecular quenching
    • [24] Grøn, H., Meldal, M. and Breddam, K., Extensive comparision of the substrate preferences of two subtilisins as determined with peptide substrates which are based on the principle of intramolecular quenching. Biochemistry, 31 (1992) 6011-6018.
    • (1992) Biochemistry , vol.31 , pp. 6011-6018
    • Grøn, H.1    Meldal, M.2    Breddam, K.3
  • 25
    • 0028817280 scopus 로고
    • Internally quenched fluorogenic substrate for furin
    • [25] Angliker, H., Neumann, U., Molloy, S.S. and Thomas, J., Internally quenched fluorogenic substrate for furin. Anal. Biochem., 224 (1995) 409-412.
    • (1995) Anal. Biochem. , vol.224 , pp. 409-412
    • Angliker, H.1    Neumann, U.2    Molloy, S.S.3    Thomas, J.4
  • 26
    • 0019943988 scopus 로고
    • Fluorogenic substrates for bacterial aminopeptidase P and its analogs detected in human serum and culf lung
    • [26] Fleminger, G., Carmel, A., Goldenberg, D. and Yaron, A., Fluorogenic substrates for bacterial aminopeptidase P and its analogs detected in human serum and culf lung. Eur. J. Biochem., 125 (1982) 609-615.
    • (1982) Eur. J. Biochem. , vol.125 , pp. 609-615
    • Fleminger, G.1    Carmel, A.2    Goldenberg, D.3    Yaron, A.4
  • 27
    • 0023193617 scopus 로고
    • Aminopeptidase P activity in rat organs and human serum
    • [27] Holtzman, E.I., Pilay, G., Rosenthal, T. and Yaron, A., Aminopeptidase P activity in rat organs and human serum. Anal. Biochem., 162 (1987) 476-484.
    • (1987) Anal. Biochem. , vol.162 , pp. 476-484
    • Holtzman, E.I.1    Pilay, G.2    Rosenthal, T.3    Yaron, A.4
  • 28
    • 0026637720 scopus 로고
    • Kinase activity in human plateles: Cleavage of the Arg-Pro bond of bradykinin by aminopeptidase P
    • [28] Vanhoof, G., De Meester, I., Goossens, F., Hendriks, D., Scharpe, S. and Yaron, A., Kinase activity in human plateles: cleavage of the Arg-Pro bond of bradykinin by aminopeptidase P. Biochem. Pharmacol., 44 (1992) 479-487.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 479-487
    • Vanhoof, G.1    De Meester, I.2    Goossens, F.3    Hendriks, D.4    Scharpe, S.5    Yaron, A.6
  • 30
    • 0023735860 scopus 로고
    • Continuous fluorogenic substrates for atrial dipeptidyl carboxypeeptidase
    • [30] Soler, D.F. and Harris, R.B., Continuous fluorogenic substrates for atrial dipeptidyl carboxypeeptidase. Int. J. Pept. Protein Res., 32 (1988) 35-40.
    • (1988) Int. J. Pept. Protein Res. , vol.32 , pp. 35-40
    • Soler, D.F.1    Harris, R.B.2
  • 31
    • 0025663423 scopus 로고
    • A simple, continuous fluometric assay for HIV protease
    • [31] Toth, M.V. and Marshall, G.R., A simple, continuous fluometric assay for HIV protease. Int. J. Pept. Protein Res., 36 (1990) 544-550.
    • (1990) Int. J. Pept. Protein Res. , vol.36 , pp. 544-550
    • Toth, M.V.1    Marshall, G.R.2
  • 32
    • 0019891696 scopus 로고
    • Use of an intramolecularly quenched fluorogenic substrate for study of a thiol-dependent acidic dipeptidyl carboxypeptidase in cellular extracts and in living cells
    • [32] Fleminger, G., Goldenberg, D. and Yaron, A., Use of an intramolecularly quenched fluorogenic substrate for study of a thiol-dependent acidic dipeptidyl carboxypeptidase in cellular extracts and in living cells. FEBS Lett., 135 (1981) 131-134.
    • (1981) FEBS Lett. , vol.135 , pp. 131-134
    • Fleminger, G.1    Goldenberg, D.2    Yaron, A.3
  • 33
    • 0021137049 scopus 로고
    • A highly sensitive fluometric assay for 'enkephalinase', a neutral metalloendopeptidase that releases tyrosine-glycine from enkephalins
    • [33] Florentin, D., Sassi, A. and Raques, B.P., A highly sensitive fluometric assay for 'enkephalinase', a neutral metalloendopeptidase that releases tyrosine-glycine from enkephalins. Anal. Biochem., 141 (1984) 62-69.
    • (1984) Anal. Biochem. , vol.141 , pp. 62-69
    • Florentin, D.1    Sassi, A.2    Raques, B.P.3
  • 34
    • 0023655833 scopus 로고
    • Chromophoric and fluorophoric peptide substrates cleaved through the dipeptidyl carboxypeptidase activity of cathepsin B
    • [34] Pohl, J., Davinic, S., Blaha, I., Strop, P. and Kostka, V., Chromophoric and fluorophoric peptide substrates cleaved through the dipeptidyl carboxypeptidase activity of cathepsin B. Anal. Biochem., 165 (1987) 96-101.
    • (1987) Anal. Biochem. , vol.165 , pp. 96-101
    • Pohl, J.1    Davinic, S.2    Blaha, I.3    Strop, P.4    Kostka, V.5
  • 35
    • 0020727553 scopus 로고
    • A new substrate for porcine pepsin possessing cryptic fluorescence properties
    • [35] Deurup, C. and Dunn, B.M., A new substrate for porcine pepsin possessing cryptic fluorescence properties. Anal. Biochem., 129 (1983) 502-512.
    • (1983) Anal. Biochem. , vol.129 , pp. 502-512
    • Deurup, C.1    Dunn, B.M.2
  • 36
    • 0017718623 scopus 로고
    • A fluorogenic substrate for anginotensin converting enzyme
    • [36] Persson, A. and Wilson, I.B., A fluorogenic substrate for anginotensin converting enzyme. Anal. Biochem., 83 (1977) 296-309.
    • (1977) Anal. Biochem. , vol.83 , pp. 296-309
    • Persson, A.1    Wilson, I.B.2
  • 37
    • 0018387211 scopus 로고
    • A fluometric assay for anginotensin-1-converting enzyme in human serum
    • [37] Carmel, A., Ehrlich-Rogozinsky, S. and Yaron. A., A fluometric assay for anginotensin-1-converting enzyme in human serum. Clin. Chim. Acta, 93 (1979) 215-220.
    • (1979) Clin. Chim. Acta , vol.93 , pp. 215-220
    • Carmel, A.1    Ehrlich-Rogozinsky, S.2    Yaron, A.3
  • 38
    • 0023742672 scopus 로고
    • Organic fluorescent reagent. XIV. Novel fluorogenic substrates for microdetermination of chimotrypsin and aminopeptidase: Bimane fluorescence appears after hydrolysis
    • [38] Sato, E., Sakashita, M., Kanaoka, Y. and Kosower, E.M.. Organic fluorescent reagent. XIV. Novel fluorogenic substrates for microdetermination of chimotrypsin and aminopeptidase: bimane fluorescence appears after hydrolysis. Bioorg. Chem., 16 (1988) 298-306.
    • (1988) Bioorg. Chem. , vol.16 , pp. 298-306
    • Sato, E.1    Sakashita, M.2    Kanaoka, Y.3    Kosower, E.M.4
  • 39
    • 0025737677 scopus 로고
    • Bimane fluorogenic substrates for microdetermination of anginotensin converting enzyme level in serum
    • [39] Sato, E., Hattori, H.. Nishikawa, S. and Kanaoka, Y., Bimane fluorogenic substrates for microdetermination of anginotensin converting enzyme level in serum. Chem. Pharm. Bull., 39 (1991) 2146-2148.
    • (1991) Chem. Pharm. Bull. , vol.39 , pp. 2146-2148
    • Sato, E.1    Hattori, H.2    Nishikawa, S.3    Kanaoka, Y.4
  • 40
    • 0024266347 scopus 로고
    • New fluorogenic substrates for microdetermination of carboxypeptidase A
    • [40] Sato, E. and Kanaoka, Y., new fluorogenic substrates for microdetermination of carboxypeptidase A. Chem. Pharm. Bull., 36 (1988) 4494-4498.
    • (1988) Chem. Pharm. Bull. , vol.36 , pp. 4494-4498
    • Sato, E.1    Kanaoka, Y.2
  • 41
    • 0024555771 scopus 로고
    • Novel fluorogenic substrates containing bimane system for microdetermination of anginotensin-1-converting enzyme level in serum
    • [41] Sato, E., Nishikawa, S. and Kanaoka, Y., Novel fluorogenic substrates containing bimane system for microdetermination of anginotensin-1-converting enzyme level in serum. Chem. Pharm. Bull., 37 (1989) 145-147.
    • (1989) Chem. Pharm. Bull. , vol.37 , pp. 145-147
    • Sato, E.1    Nishikawa, S.2    Kanaoka, Y.3
  • 42
    • 0024991192 scopus 로고
    • New fluorogenic substrates for microdetermination of cathepsin C
    • [42] Sato, E., Matsuda, K. and Kanaoka, Y., New fluorogenic substrates for microdetermination of cathepsin C. Chem. Pharm. Bull., 38 (1990) 2043-2044.
    • (1990) Chem. Pharm. Bull. , vol.38 , pp. 2043-2044
    • Sato, E.1    Matsuda, K.2    Kanaoka, Y.3
  • 43
    • 0015424260 scopus 로고
    • Fluorescence determination of carboxypeptidase activity based on electronic energy transfer
    • [43] Latt, S.A., Auld, D.S. and Vallee, B.L., Fluorescence determination of carboxypeptidase activity based on electronic energy transfer. Anal. Biochem., 50 (1972) 56-62.
    • (1972) Anal. Biochem. , vol.50 , pp. 56-62
    • Latt, S.A.1    Auld, D.S.2    Vallee, B.L.3
  • 44
    • 0025259099 scopus 로고
    • Fluorescence-based continuous assay for the aspartyl protease of human immunodeficiency virus-1
    • [44] Geoghegan, K.F., Spencer, R.W., Danley, D.E., Contillo, L.G. and Andrews, G.C., Fluorescence-based continuous assay for the aspartyl protease of human immunodeficiency virus-1. FEBS Lett., 262 (1990) 119-122.
    • (1990) FEBS Lett. , vol.262 , pp. 119-122
    • Geoghegan, K.F.1    Spencer, R.W.2    Danley, D.E.3    Contillo, L.G.4    Andrews, G.C.5
  • 45
    • 0011365147 scopus 로고
    • Fluorogenic substrate of pepsin
    • [45] Yanezawa, H. and Izumiya, N., Fluorogenic substrate of pepsin. Bull. Chem. Soc. Jpn., 64 (1991) 1407-1409.
    • (1991) Bull. Chem. Soc. Jpn. , vol.64 , pp. 1407-1409
    • Yanezawa, H.1    Izumiya, N.2
  • 48
    • 0023140942 scopus 로고
    • New substrates for enkephalynase (neutral endopeptidase) based on fluorescence energy transfer
    • [48] Malfrog, B. and Burnier, J., New substrates for enkephalynase (neutral endopeptidase) based on fluorescence energy transfer. Biochem. Biophys. Res. Commun., 143 (1987) 58-66.
    • (1987) Biochem. Biophys. Res. Commun. , vol.143 , pp. 58-66
    • Malfrog, B.1    Burnier, J.2
  • 49
    • 0024330806 scopus 로고
    • A fluorescent oligopeptide energy transfer assay with broad application for neutral proteases
    • [49] Ng. M, and Auld, D.S., A fluorescent oligopeptide energy transfer assay with broad application for neutral proteases. Anal. Biochem., 183 (1989) 50-56.
    • (1989) Anal. Biochem. , vol.183 , pp. 50-56
    • Ng, M.1    Auld, D.S.2
  • 50
    • 0025717986 scopus 로고
    • A fluorescence assay for endothelin-converting enzyme
    • [50] Von Geldren, W.T., Holleman, W.H. and Opgenorth, T.J., A fluorescence assay for endothelin-converting enzyme. Peptide Res., 4 (1991) 32-35.
    • (1991) Peptide Res. , vol.4 , pp. 32-35
    • Von Geldren, W.T.1    Holleman, W.H.2    Opgenorth, T.J.3
  • 51
    • 0026784268 scopus 로고
    • FMOC solid phase synthesis of an endothelin converting enzyme substrate
    • [51] Handa, B.K. and Keech, E., FMOC solid phase synthesis of an endothelin converting enzyme substrate. Int. J. Pept. Protein Res., 40 (1992) 66-71.
    • (1992) Int. J. Pept. Protein Res. , vol.40 , pp. 66-71
    • Handa, B.K.1    Keech, E.2
  • 52
    • 0025915082 scopus 로고
    • Continuously recording fluorescent assays optimized for five human matrix metalloproteinases
    • [52] Netzel-Arnett. S., Mallya, S.K., Nagase. H., Birkedal-Hansen, H. and Van Wart, H.E., Continuously recording fluorescent assays optimized for five human matrix metalloproteinases. Anal. Biochem., 195 (1991) 86-92.
    • (1991) Anal. Biochem. , vol.195 , pp. 86-92
    • Netzel-Arnett, S.1    Mallya, S.K.2    Nagase, H.3    Birkedal-Hansen, H.4    Van Wart, H.E.5
  • 53
    • 0024564708 scopus 로고
    • Comparison of vertebrate collagenase and gelatinase using a new fluorogenic substrate peptide
    • [53] Stack. M.S. and Gray, R.D., Comparison of vertebrate collagenase and gelatinase using a new fluorogenic substrate peptide. J. Biol. Chem., 264 (1989) 4277-4281.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4277-4281
    • Stack, M.S.1    Gray, R.D.2
  • 54
    • 0027050785 scopus 로고
    • Substrate specificity of the human matrix metalloproteinase stromelysin and the development of continuous fluometric assays
    • [54] Niedzwiecki, E., Teahan, J., Harrison, R.K. and Stein. R.L., Substrate specificity of the human matrix metalloproteinase stromelysin and the development of continuous fluometric assays. Biochemistry, 31 (1992) 12618-12623.
    • (1992) Biochemistry , vol.31 , pp. 12618-12623
    • Niedzwiecki, E.1    Teahan, J.2    Harrison, R.K.3    Stein, R.L.4
  • 57
    • 0011332088 scopus 로고
    • 2-Aminobenzoyl-peptide-2,4-dinitroanilinoethylamides. Facile fluorescent detection system for sequence specific proteases
    • [57] Nishino, N., Makinose, Y. and Fujimoto, T., 2-Aminobenzoyl-peptide-2,4-dinitroanilinoethylamides. Facile fluorescent detection system for sequence specific proteases. Chem. Lett., 1 (1992) 77-80.
    • (1992) Chem. Lett. , vol.1 , pp. 77-80
    • Nishino, N.1    Makinose, Y.2    Fujimoto, T.3
  • 61
    • 0025363494 scopus 로고
    • An alternative quenched fluorescence substrate for Pz-peptidase
    • [61] Tisljiar, U., Knight, C.G. and Barret, A.J., An alternative quenched fluorescence substrate for Pz-peptidase. Anal. Biochem., 186 (1990) 112-115.
    • (1990) Anal. Biochem. , vol.186 , pp. 112-115
    • Tisljiar, U.1    Knight, C.G.2    Barret, A.J.3
  • 62
    • 0025981265 scopus 로고
    • A quenched fluorescent substrate for thimet peptidase containing a new fluorescent amino acid, D,L-2-amino-3-(7-methoxy-4-coumaryl)propionic acid
    • [62] Knight, C.G., A quenched fluorescent substrate for thimet peptidase containing a new fluorescent amino acid, D,L-2-amino-3-(7-methoxy-4-coumaryl)propionic acid. Biochem. J., 274 (1991) 45-48.
    • (1991) Biochem. J. , vol.274 , pp. 45-48
    • Knight, C.G.1
  • 63
    • 0026505650 scopus 로고
    • A novel coumarin-labelled peptide for sensitivy continuous assays of the matrix metalloproteinases
    • [63] Knight, C.G., Willenbrock, F. and Murphy, G., A novel coumarin-labelled peptide for sensitivy continuous assays of the matrix metalloproteinases. FEBS Lett., 296 (1992) 263-266.
    • (1992) FEBS Lett. , vol.296 , pp. 263-266
    • Knight, C.G.1    Willenbrock, F.2    Murphy, G.3
  • 64
    • 37049074547 scopus 로고
    • Synthesis and study of intramolecularly-quenched fluorogenic substrates, containing aminocoumarin-type fluorophores
    • [64] Kokotos, G. and Tzougraki, Ch., Synthesis and study of intramolecularly-quenched fluorogenic substrates, containing aminocoumarin-type fluorophores. J. Chem. Soc., Perkin Trans., part 2, 4 (1991) 495-499.
    • (1991) J. Chem. Soc., Perkin Trans. , vol.4 , Issue.PART 2 , pp. 495-499
    • Kokotos, G.1    Tzougraki, Ch.2
  • 65
    • 0025918740 scopus 로고
    • Fluorogenic bimane substrate with dabsyl group for endopeptidases: Chymotrypsin, collagenase and thermolysin
    • [65] Sato, E., Hattori, H. and Kanaoka, Y., Fluorogenic bimane substrate with DABSYL group for endopeptidases: chymotrypsin, collagenase and thermolysin. J. Pharmacobiodyn., 14 (1991) 599-604.
    • (1991) J. Pharmacobiodyn. , vol.14 , pp. 599-604
    • Sato, E.1    Hattori, H.2    Kanaoka, Y.3
  • 66
    • 0002475102 scopus 로고
    • Use of substrates with fluorescent donor and acceptor chromophores for the kinetic assay of hydrolases
    • [66] Carmel. A., Zur, M.. Yaron, A. and Katchalski, E., Use of substrates with fluorescent donor and acceptor chromophores for the kinetic assay of hydrolases. FEBS Lett., 30 (1973) 11-14.
    • (1973) FEBS Lett. , vol.30 , pp. 11-14
    • Carmel, A.1    Zur, M.2    Yaron, A.3    Katchalski, E.4
  • 67
    • 0025053937 scopus 로고
    • Design and synthesis of new fluorogenic HIV protease substrates based on resonance energy transfer
    • [67] Wang, G.T., Matagoshi, E., Huffaker, H.J. and Kraft, G.A., Design and synthesis of new fluorogenic HIV protease substrates based on resonance energy transfer. Tetrahedron Lett., 31 (1990) 6493-6496.
    • (1990) Tetrahedron Lett. , vol.31 , pp. 6493-6496
    • Wang, G.T.1    Matagoshi, E.2    Huffaker, H.J.3    Kraft, G.A.4
  • 68
    • 0025099455 scopus 로고
    • Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer
    • [68] Matayoshi, E.D., Wang, G.T., Kraft, G.A. and Erickson, J., Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer. Science, 247 (1990) 954-958.
    • (1990) Science , vol.247 , pp. 954-958
    • Matayoshi, E.D.1    Wang, G.T.2    Kraft, G.A.3    Erickson, J.4
  • 69
    • 0027289345 scopus 로고
    • A continouos fluorescence assay of renin activity
    • [69] Wang. G.T., Chung, C.C., Holzman, T.F. and Kraft. J.A.. A continouos fluorescence assay of renin activity. Anal. Biochem., 210 (1993) 351-359.
    • (1993) Anal. Biochem. , vol.210 , pp. 351-359
    • Wang, G.T.1    Chung, C.C.2    Holzman, T.F.3    Kraft, J.A.4
  • 70
    • 0028121382 scopus 로고
    • Synthesis of a fluorogenic interleukin-1β-converting enzyme substrate based on resonance energy transfer
    • [70] Pennington. M.W. and Thornberry, N.A., Synthesis of a fluorogenic interleukin-1β-converting enzyme substrate based on resonance energy transfer. Pept. Res., 7 (1994) 72-76.
    • (1994) Pept. Res. , vol.7 , pp. 72-76
    • Pennington, M.W.1    Thornberry, N.A.2
  • 71
    • 0026503894 scopus 로고
    • New intramolecularly fluorogenic peptide substrates for the study of the kinetic specificity of papain
    • [71] Garcia-Echeverria, C. and Rich, D.H., New intramolecularly fluorogenic peptide substrates for the study of the kinetic specificity of papain. FEBS Lett., 297 (1992) 100-102.
    • (1992) FEBS Lett. , vol.297 , pp. 100-102
    • Garcia-Echeverria, C.1    Rich, D.H.2
  • 72
    • 0026680191 scopus 로고
    • Application of a fluorogenic substrate in the assay of proteolytic activity and in the discovery of a potent inhibitor of Candida albicans aspartic proteinase
    • [72] Capobianco, J.O., Lerner, C.G. and Goldman, R.C., Application of a fluorogenic substrate in the assay of proteolytic activity and in the discovery of a potent inhibitor of Candida albicans aspartic proteinase. Anal. Biochem., 204 (1992) 96-102.
    • (1992) Anal. Biochem. , vol.204 , pp. 96-102
    • Capobianco, J.O.1    Lerner, C.G.2    Goldman, R.C.3
  • 74
    • 0026483377 scopus 로고
    • A general method for the preparation of internally quenched fluorogenic protease substrates using solid-phase peptide synthesis
    • [74] Maggiera, L.L., Smith, C.W. and Zhang, Z.-Y.. A general method for the preparation of internally quenched fluorogenic protease substrates using solid-phase peptide synthesis. J. Med. Chem., 35 (1992) 3727-3730.
    • (1992) J. Med. Chem. , vol.35 , pp. 3727-3730
    • Maggiera, L.L.1    Smith, C.W.2    Zhang, Z.-Y.3
  • 76
    • 0028992812 scopus 로고
    • The intrinsic fluorescence upon the hydrolysis of tyrosine peptides: Application to proteinase assays
    • [76] Peranteau, A.G., Kuzmic, P., Angell, Y., Garcia-Echeverria, C. and Rich, D.H., The intrinsic fluorescence upon the hydrolysis of tyrosine peptides: Application to proteinase assays. Anal. Biochem., 227 (1995) 242-245.
    • (1995) Anal. Biochem. , vol.227 , pp. 242-245
    • Peranteau, A.G.1    Kuzmic, P.2    Angell, Y.3    Garcia-Echeverria, C.4    Rich, D.H.5
  • 77
    • 0011292474 scopus 로고
    • Synthesis and characterization of fluorogenic substrate of HIV-1 protease based on fluorescence resonance energy transfer
    • [77] Kornelyuk, A.I., Terentiev, A.G., Fisher, S. and Porter, T., Synthesis and characterization of fluorogenic substrate of HIV-1 protease based on fluorescence resonance energy transfer. Biopolymery i kletka. 11 (1995) 56-60.
    • (1995) Biopolymery I Kletka. , vol.11 , pp. 56-60
    • Kornelyuk, A.I.1    Terentiev, A.G.2    Fisher, S.3    Porter, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.