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Volumn 52, Issue 3, 2010, Pages 355-361

Development of a liquid chromatographic system with fluorescent detection for β-secretase immobilized enzyme reactor on-line enzymatic studies

Author keywords

Fluorescence detection; hrBACE1 IMER; Inhibitors screening; Methoxycoumaryl peptide substrate

Indexed keywords

AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; GALLOCATECHIN; M 2420; OM 99 2; PANVERA PEPTIDE; PEPSTATIN; PEPTIDOMIMETIC AGENT; POLYPHENOL; STATIN PEPTIDE; UNCLASSIFIED DRUG;

EID: 77649180890     PISSN: 07317085     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jpba.2009.07.012     Document Type: Article
Times cited : (18)

References (34)
  • 1
    • 0033613129 scopus 로고    scopus 로고
    • Cellular mechanisms of beta-amyloid production and secretion
    • Sinha S., and Lieberburg I. Cellular mechanisms of beta-amyloid production and secretion. Proc. Natl. Acad. Sci. U S A 96 (1999) 11049-11053
    • (1999) Proc. Natl. Acad. Sci. U S A , vol.96 , pp. 11049-11053
    • Sinha, S.1    Lieberburg, I.2
  • 2
    • 57649217285 scopus 로고    scopus 로고
    • The role of amyloid precursor protein processing by BACE1, the beta-secretase, in Alzheimer disease pathophysiology
    • Cole S.L., and Vassar R. The role of amyloid precursor protein processing by BACE1, the beta-secretase, in Alzheimer disease pathophysiology. J. Biol. Chem. 283 (2008) 29621-29625
    • (2008) J. Biol. Chem. , vol.283 , pp. 29621-29625
    • Cole, S.L.1    Vassar, R.2
  • 3
    • 38349107593 scopus 로고    scopus 로고
    • The Alzheimer's disease beta-secretase enzyme, BACE1
    • Cole S.L., and Vassar R. The Alzheimer's disease beta-secretase enzyme, BACE1. Mol. Neurodegener. 2 (2007) 22-46
    • (2007) Mol. Neurodegener. , vol.2 , pp. 22-46
    • Cole, S.L.1    Vassar, R.2
  • 4
    • 33745052352 scopus 로고    scopus 로고
    • Development of BACE1 inhibitors for Alzheimer's disease
    • Guo T., and Hobbs D.W. Development of BACE1 inhibitors for Alzheimer's disease. Curr. Med. Chem. 13 (2006) 1811-1829
    • (2006) Curr. Med. Chem. , vol.13 , pp. 1811-1829
    • Guo, T.1    Hobbs, D.W.2
  • 5
    • 62249167406 scopus 로고    scopus 로고
    • Boom in the development of non-peptidic beta-secretase (BACE1) inhibitors for the treatment of Alzheimer's disease
    • Silvestri R. Boom in the development of non-peptidic beta-secretase (BACE1) inhibitors for the treatment of Alzheimer's disease. Med. Res. Rev. 2 (2009) 295-338
    • (2009) Med. Res. Rev. , vol.2 , pp. 295-338
    • Silvestri, R.1
  • 8
    • 0038729338 scopus 로고    scopus 로고
    • Measuring human beta-secretase (BACE1) activity using homogeneous time-resolved fluorescence
    • Kennedy M.E., Wang W., Song L., Lee J., Zhang L., Wong G., Wang L., and Parker E. Measuring human beta-secretase (BACE1) activity using homogeneous time-resolved fluorescence. Anal. Biochem. 319 (2003) 49-55
    • (2003) Anal. Biochem. , vol.319 , pp. 49-55
    • Kennedy, M.E.1    Wang, W.2    Song, L.3    Lee, J.4    Zhang, L.5    Wong, G.6    Wang, L.7    Parker, E.8
  • 10
    • 0041842684 scopus 로고    scopus 로고
    • Effect of detergent on "promiscuous" inhibitors
    • Ryan A.J., Gray N.M., Lowe P.N., and Chung C. Effect of detergent on "promiscuous" inhibitors. J. Med. Chem. 46 (2003) 3448-3451
    • (2003) J. Med. Chem. , vol.46 , pp. 3448-3451
    • Ryan, A.J.1    Gray, N.M.2    Lowe, P.N.3    Chung, C.4
  • 12
    • 51249111291 scopus 로고    scopus 로고
    • Development of immobilized enzyme reactors based on human recombinant cytochrome P450 enzymes for phase I drug metabolism studies
    • Nicoli R., Bartolini M., Rudaz S., Andrisano V., and Veuthey J.L. Development of immobilized enzyme reactors based on human recombinant cytochrome P450 enzymes for phase I drug metabolism studies. J. Chromatogr. A 1206 (2008) 2-10
    • (2008) J. Chromatogr. A , vol.1206 , pp. 2-10
    • Nicoli, R.1    Bartolini, M.2    Rudaz, S.3    Andrisano, V.4    Veuthey, J.L.5
  • 13
    • 13844280985 scopus 로고    scopus 로고
    • Choosing the right chromatographic support in making a new acetylcholinesterase-micro-immobilised enzyme reactor for drug discovery
    • Bartolini M., Cavrini V., and Andrisano V. Choosing the right chromatographic support in making a new acetylcholinesterase-micro-immobilised enzyme reactor for drug discovery. J. Chromatogr. A 1065 (2005) 135-144
    • (2005) J. Chromatogr. A , vol.1065 , pp. 135-144
    • Bartolini, M.1    Cavrini, V.2    Andrisano, V.3
  • 14
    • 0036499743 scopus 로고    scopus 로고
    • Biosynthesis in an on-line immobilized-enzyme reactor containing phenylethanolamine N-methyltransferase in single-enzyme and coupled-enzyme formats
    • Markoglou N., and Wainer I.W. Biosynthesis in an on-line immobilized-enzyme reactor containing phenylethanolamine N-methyltransferase in single-enzyme and coupled-enzyme formats. J. Chromatogr. A 948 (2002) 249-256
    • (2002) J. Chromatogr. A , vol.948 , pp. 249-256
    • Markoglou, N.1    Wainer, I.W.2
  • 15
    • 37249083034 scopus 로고    scopus 로고
    • The development of an immobilized enzyme reactor containing glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi: the effect of species' specific differences on the immobilization
    • Cardoso C.L., de Moraes M.C., Guido R.V., Oliva G., Andricopulo A.D., Wainer I.W., and Cass Q.B. The development of an immobilized enzyme reactor containing glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi: the effect of species' specific differences on the immobilization. Analyst 133 (2008) 93-99
    • (2008) Analyst , vol.133 , pp. 93-99
    • Cardoso, C.L.1    de Moraes, M.C.2    Guido, R.V.3    Oliva, G.4    Andricopulo, A.D.5    Wainer, I.W.6    Cass, Q.B.7
  • 16
    • 37549012988 scopus 로고    scopus 로고
    • Initial synthesis and characterization of an immobilized heat shock protein 90 column for online determination of binding affinities
    • Marszałł M.P., Moaddel R., Jozwiak K., Bernier M., and Wainer I.W. Initial synthesis and characterization of an immobilized heat shock protein 90 column for online determination of binding affinities. Anal. Biochem. 373 (2008) 313-321
    • (2008) Anal. Biochem. , vol.373 , pp. 313-321
    • Marszałł, M.P.1    Moaddel, R.2    Jozwiak, K.3    Bernier, M.4    Wainer, I.W.5
  • 17
    • 23644445337 scopus 로고    scopus 로고
    • The covalent immobilization of microsomal uridine diphospho-glucuronosyltransferase (UDPGT): initial synthesis and characterization of an UDPGT immobilized enzyme reactor for the on-line study of glucuronidation
    • Kim H.S., and Wainer I.W. The covalent immobilization of microsomal uridine diphospho-glucuronosyltransferase (UDPGT): initial synthesis and characterization of an UDPGT immobilized enzyme reactor for the on-line study of glucuronidation. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 823 (2005) 158-166
    • (2005) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.823 , pp. 158-166
    • Kim, H.S.1    Wainer, I.W.2
  • 19
    • 4344652819 scopus 로고    scopus 로고
    • Development of a chromatographic bioreactor based on immobilized beta-glucuronidase on monolithic support for the determination of dextromethorphan and dextrorphan in human urine
    • Calleri E., Marrubini G., Massolini G., Lubda D., de Fazio S.S., Furlanetto S., Wainer I.W., Manzo L., and Caccialanza G. Development of a chromatographic bioreactor based on immobilized beta-glucuronidase on monolithic support for the determination of dextromethorphan and dextrorphan in human urine. J. Pharm. Biomed. Anal. 35 (2004) 1179-1189
    • (2004) J. Pharm. Biomed. Anal. , vol.35 , pp. 1179-1189
    • Calleri, E.1    Marrubini, G.2    Massolini, G.3    Lubda, D.4    de Fazio, S.S.5    Furlanetto, S.6    Wainer, I.W.7    Manzo, L.8    Caccialanza, G.9
  • 20
    • 61449149521 scopus 로고    scopus 로고
    • Immobilized butyrylcholinesterase in the characterization of new inhibitors that could ease Alzheimer's disease
    • Bartolini M., Greig N.H., Yu Q.S., and Andrisano V. Immobilized butyrylcholinesterase in the characterization of new inhibitors that could ease Alzheimer's disease. J. Chromatogr. A 1216 (2009) 2730-2738
    • (2009) J. Chromatogr. A , vol.1216 , pp. 2730-2738
    • Bartolini, M.1    Greig, N.H.2    Yu, Q.S.3    Andrisano, V.4
  • 21
    • 36549089033 scopus 로고    scopus 로고
    • Development and characterization of beta-secretase monolithic micro-immobilized enzyme reactor for on-line high-performance liquid chromatography studies
    • Mancini F., Naldi M., Cavrini V., and Andrisano V. Development and characterization of beta-secretase monolithic micro-immobilized enzyme reactor for on-line high-performance liquid chromatography studies. J. Chromatogr. A 1175 (2007) 217-226
    • (2007) J. Chromatogr. A , vol.1175 , pp. 217-226
    • Mancini, F.1    Naldi, M.2    Cavrini, V.3    Andrisano, V.4
  • 23
    • 4744366997 scopus 로고    scopus 로고
    • Highly sensitive intramolecularly quenched fluorogenic substrates for renin based on the combination of L-2-amino-3-(7-methoxy-4-coumaryl)propionic acid with 2,4-dinitrophenyl groups at various positions
    • Paschalidou K., Neumann U., Gerharts B., and Tzougraki C. Highly sensitive intramolecularly quenched fluorogenic substrates for renin based on the combination of L-2-amino-3-(7-methoxy-4-coumaryl)propionic acid with 2,4-dinitrophenyl groups at various positions. Biochem. J. 382 (2004) 1031-1038
    • (2004) Biochem. J. , vol.382 , pp. 1031-1038
    • Paschalidou, K.1    Neumann, U.2    Gerharts, B.3    Tzougraki, C.4
  • 24
    • 67651047153 scopus 로고    scopus 로고
    • Progress in the development of nonpeptidomimetic BACE 1 inhibitors for Alzheimer's disease
    • Huang W.H., Sheng R., and Hu Y.Z. Progress in the development of nonpeptidomimetic BACE 1 inhibitors for Alzheimer's disease. Curr. Med. Chem. 16 (2009) 1806-1820
    • (2009) Curr. Med. Chem. , vol.16 , pp. 1806-1820
    • Huang, W.H.1    Sheng, R.2    Hu, Y.Z.3
  • 25
    • 63949088562 scopus 로고    scopus 로고
    • Function, regulation and therapeutic properties of beta-secretase (BACE1)
    • Willem M., Lammich S., and Haass C. Function, regulation and therapeutic properties of beta-secretase (BACE1). Semin. Cell. Dev. Biol. 20 (2009) 175-182
    • (2009) Semin. Cell. Dev. Biol. , vol.20 , pp. 175-182
    • Willem, M.1    Lammich, S.2    Haass, C.3
  • 27
    • 0034633995 scopus 로고    scopus 로고
    • Proteolytic activation of recombinant pro-memapsin 2 (pro-beta-secretase) studied with new fluorogenic substrates
    • Ermolieff J., Loy J.A., Koelsch G., and Tang J. Proteolytic activation of recombinant pro-memapsin 2 (pro-beta-secretase) studied with new fluorogenic substrates. Biochemistry 39 (2000) 12450-12456
    • (2000) Biochemistry , vol.39 , pp. 12450-12456
    • Ermolieff, J.1    Loy, J.A.2    Koelsch, G.3    Tang, J.4
  • 28
    • 0022799189 scopus 로고
    • The determination of specificity constants in enzyme-catalysed reactions
    • Crompton I.E., and Waley S.G. The determination of specificity constants in enzyme-catalysed reactions. Biochem. J. 239 (1986) 221-224
    • (1986) Biochem. J. , vol.239 , pp. 221-224
    • Crompton, I.E.1    Waley, S.G.2
  • 29
    • 34547333504 scopus 로고    scopus 로고
    • Multiwell fluorometric and colorimetric microassays for the evaluation of beta-secretase (BACE-1) inhibitors
    • Mancini F., Naldi M., Cavrini V., and Andrisano V. Multiwell fluorometric and colorimetric microassays for the evaluation of beta-secretase (BACE-1) inhibitors. Anal. Biochem. 388 (2007) 1175-1183
    • (2007) Anal. Biochem. , vol.388 , pp. 1175-1183
    • Mancini, F.1    Naldi, M.2    Cavrini, V.3    Andrisano, V.4
  • 31
    • 0034721842 scopus 로고    scopus 로고
    • Maturation and endosomal targeting of beta-site amyloid precursor protein-cleaving enzyme. The Alzheimer's disease beta-secretase
    • Huse J.T., Pijak D.S., Leslie G.J., Lee V.M., and Doms R.V. Maturation and endosomal targeting of beta-site amyloid precursor protein-cleaving enzyme. The Alzheimer's disease beta-secretase. J. Biol. Chem. 275 (2000) 33729-33737
    • (2000) J. Biol. Chem. , vol.275 , pp. 33729-33737
    • Huse, J.T.1    Pijak, D.S.2    Leslie, G.J.3    Lee, V.M.4    Doms, R.V.5
  • 32
    • 0242285619 scopus 로고    scopus 로고
    • Green tea catechins as a BACE1 (beta-secretase) inhibitor
    • Jeon S.Y., Bae K., Seong Y.H., and Song K.S. Green tea catechins as a BACE1 (beta-secretase) inhibitor. Bioorg. Med. Chem. Lett. 13 (2003) 3905-3908
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 3905-3908
    • Jeon, S.Y.1    Bae, K.2    Seong, Y.H.3    Song, K.S.4
  • 33
    • 0037085353 scopus 로고    scopus 로고
    • Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases
    • Grüninger-Leitch F., Schlatter D., Küng E., Nelböck P., and Döbeli H. Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases. J. Biol. Chem. 277 (2002) 4687-4893
    • (2002) J. Biol. Chem. , vol.277 , pp. 4687-4893
    • Grüninger-Leitch, F.1    Schlatter, D.2    Küng, E.3    Nelböck, P.4    Döbeli, H.5


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