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Volumn 20, Issue 11, 2009, Pages 2098-2105

Expedited solid-phase synthesis of fluorescently labeled and biotinylated aminoalkane diphenyl phosphonate affinity probes for chymotrypsin- and elastase-like serine proteases

Author keywords

[No Author keywords available]

Indexed keywords

5 [(2 AMINOETHYL)AMINO]NAPHTHALENE 1 SULFONIC ACID SUCCINYLPHENYLALANINE DIPHENYL PHOSPHONATE; 7 AMINO 4 METHYLCOUMARIN; AMINOALKANE DIPHENYL PHOSPHONATE; BIOTINYL POLYETHYLENE GLYCOL SUCCINYLPHENYLALANINE DIPHENYLPHOSPHONATE; BIOTINYL POLYETHYLENE GLYCOL SUCCINYLVALINE DIPHENYL PHOSPHONATE; CATHEPSIN G; CHYMOTRYPSIN; COUMARIN DERIVATIVE; ELASTASE LIKE SERINE PROTEASE; FLUORESCENT DYE; LEUKOCYTE ELASTASE; MUCD PEPTIDASE; SERINE PROTEINASE; STREPTAVIDIN; UNCLASSIFIED DRUG;

EID: 71249111066     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc9002162     Document Type: Article
Times cited : (12)

References (29)
  • 1
    • 7244245762 scopus 로고    scopus 로고
    • Finishing the euchromatic sequence of the human genome
    • International Human Genome Sequencing Consortium
    • International Human Genome Sequencing Consortium (2004) Finishing the euchromatic sequence of the human genome. Nature 431, 931-945.
    • (2004) Nature , vol.431 , pp. 931-945
  • 3
    • 29144531173 scopus 로고    scopus 로고
    • The druggable genome: An update
    • Russ, A. P., and Lampel, S. (2005) The druggable genome: an update. Drug Discovery Today 10, 1607-1610.
    • (2005) Drug Discovery Today , vol.10 , pp. 1607-1610
    • Russ, A.P.1    Lampel, S.2
  • 4
    • 0035827339 scopus 로고    scopus 로고
    • A genomic perspective on human proteases
    • Southan, C. (2001) A genomic perspective on human proteases. FEBS Lett. 498, 214-218.
    • (2001) FEBS Lett. , vol.498 , pp. 214-218
    • Southan, C.1
  • 5
    • 0028345645 scopus 로고
    • Quantitative zymography: Detection of picogram quantities of gelatinases
    • Kleiner, D. E., and Stetler-Stevenson, W. G. (1994) Quantitative zymography: Detection of picogram quantities of gelatinases. Anal. Biochem. 218, 235-239.
    • (1994) Anal. Biochem. , vol.218 , pp. 235-239
    • Kleiner, D.E.1    Stetler-Stevenson, W.G.2
  • 6
  • 7
    • 0026545290 scopus 로고
    • The synthesis, kinetic characterization and application of biotinylated aminoacylchloromethanes for the detection of chymotrypsin and trypsin-like serine proteinases
    • Kay, G., Bailie, J. R., Halliday, I. M., Nelson, J., and Walker, B. (1992) The synthesis, kinetic characterization and application of biotinylated aminoacylchloromethanes for the detection of chymotrypsin and trypsin-like serine proteinases. Biochem. J. 283, 455-459.
    • (1992) Biochem. J. , vol.283 , pp. 455-459
    • Kay, G.1    Bailie, J.R.2    Halliday, I.M.3    Nelson, J.4    Walker, B.5
  • 8
    • 0026598289 scopus 로고
    • The synthesis, kinetic characterisation and application of a novel biotinylated affinity label for cathepsin B
    • Walker, B., Cullen, B. M., Kay, G., Halliday, I. M., McGinty, A., and Nelson, J. (1992) The synthesis, kinetic characterisation and application of a novel biotinylated affinity label for cathepsin B. Biochem. J. 283, 449-453.
    • (1992) Biochem. J. , vol.283 , pp. 449-453
    • Walker, B.1    Cullen, B.M.2    Kay, G.3    Halliday, I.M.4    McGinty, A.5    Nelson, J.6
  • 9
    • 0026510403 scopus 로고
    • The application of a novel biotinylated affinity label for the detection of a cathepsin B-like precursor produced by breast-tumour cells in culture
    • Cullen, B. M., Halliday, I. M., Kay, G., Nelson, J., and Walker, B. (1992) The application of a novel biotinylated affinity label for the detection of a cathepsin B-like precursor produced by breast-tumour cells in culture. Biochem. J. 283, 461-465.
    • (1992) Biochem. J. , vol.283 , pp. 461-465
    • Cullen, B.M.1    Halliday, I.M.2    Kay, G.3    Nelson, J.4    Walker, B.5
  • 10
    • 0037106334 scopus 로고    scopus 로고
    • Irreversible inhibition of the bacterial cysteine protease-transpeptidase sortase (SrtA) by substrate-derived affinity labels
    • Scott, C. J., McDowell, A., Martin, S. L., Lynas, J. F., Vandenbroeck, K., and Walker, B. (2002) Irreversible inhibition of the bacterial cysteine protease-transpeptidase sortase (SrtA) by substrate-derived affinity labels. Biochem. J. 366, 953-958.
    • (2002) Biochem. J. , vol.366 , pp. 953-958
    • Scott, C.J.1    McDowell, A.2    Martin, S.L.3    Lynas, J.F.4    Vandenbroeck, K.5    Walker, B.6
  • 11
    • 0025979246 scopus 로고
    • Irreversible inhibition of serine proteases by peptide derivatives of (alpha-aminoalkyl)phosphonate diphenyl esters
    • Oleksyszyn, J., and Powers, J. C. (1991) Irreversible inhibition of serine proteases by peptide derivatives of (alpha-aminoalkyl)phosphonate diphenyl esters. Biochemistry 30, 485-493.
    • (1991) Biochemistry , vol.30 , pp. 485-493
    • Oleksyszyn, J.1    Powers, J.C.2
  • 12
    • 0028512603 scopus 로고
    • Fluorescent derivatives of diphenyl [1-(N-peptidylamino) alkyl]phosphonate esters: Synthesis and use in the inhibition and cellular localization of serine proteases
    • Abuelyaman, A. S., Hudig, D., Woodard, S. L., and Powers, J. C. (1994) Fluorescent derivatives of diphenyl [1-(N-peptidylamino) alkyl]phosphonate esters: synthesis and use in the inhibition and cellular localization of serine proteases. Bioconjugate Chem. 5, 400-405.
    • (1994) Bioconjugate Chem. , vol.5 , pp. 400-405
    • Abuelyaman, A.S.1    Hudig, D.2    Woodard, S.L.3    Powers, J.C.4
  • 13
    • 0031571612 scopus 로고    scopus 로고
    • Synthesis and kinetic studies of diphenyl 1-(N- Peptidylamino) alkanephosphonate esters and their biotinylated derivatives as inhibitors of serine proteases and probes for lymphocyte granzymes
    • DOI 10.1006/abbi.1997.0231
    • Abuelyaman, A. S., Jackson, D. S., Hudig, D., Woodard, S. L., and Powers, J. C. (1997) Synthesis and kinetic studies of diphenyl 1-(N-peptidylamino) alkanephosphonate esters and their biotinylated derivatives as inhibitors of serine proteases and probes for lymphocyte granzymes. Arch. Biochem. Biophys. 344, 271-280. (Pubitemid 27344062)
    • (1997) Archives of Biochemistry and Biophysics , vol.344 , Issue.2 , pp. 271-280
    • Abuelyaman, A.S.1    Jackson, D.S.2    Hudig, D.3    Woodard, S.L.4    Powers, J.C.5
  • 14
    • 0028004689 scopus 로고
    • Identification and characterization of the cysteine and serine proteinases of the trematode, Haplometra cylindracea and determination of their haemoglobinase activity
    • Hawthorne, S. J., Halton, D. W., and Walker, B. (1994) Identification and characterisation of the cysteine and serine proteinases of the trematode, Haplometra cylindracea and determination of their haemoglobinase activity. Parasitology 108, 595-601. (Pubitemid 2093726)
    • (1994) Parasitology , vol.108 , Issue.5 , pp. 595-601
    • Hawthorne, S.J.1    Halton, D.W.2    Walker, B.3
  • 16
    • 33745752521 scopus 로고    scopus 로고
    • Synthesis, kinetic evaluation, and utilization of a biotinylated dipeptide proline diphenyl phosphonate for the disclosure of dipeptidyl peptidase IV-like serine proteases
    • DOI 10.1016/j.bbrc.2006.06.113, PII S0006291X0601429X
    • Gilmore, B. F., Carson, L., McShane, L. L., Quinn, D., Coulter, W. A., and Walker, B. (2006) Synthesis, kinetic evaluation and utilisation of a biotinylated dipeptide proline diphenyl phosphonate for the disclosure of dipeptidyl peptidase IV-like serine proteases. Biochem. Biophys. Res. Commun. 347, 373-379. (Pubitemid 44015687)
    • (2006) Biochemical and Biophysical Research Communications , vol.347 , Issue.1 , pp. 373-379
    • Gilmore, B.F.1    Carson, L.2    McShane, L.L.3    Quinn, D.4    Coulter, W.A.5    Walker, B.6
  • 17
    • 0035799319 scopus 로고    scopus 로고
    • Profiling serine hydrolase activities in complex proteomes
    • DOI 10.1021/bi002579j
    • Kidd, D., Liu, Y., and Cravatt, B. F. (2001) Profiling serine hydrolase activities in complex proteomes. Biochemistry 40, 4005-4015. (Pubitemid 32280438)
    • (2001) Biochemistry , vol.40 , Issue.13 , pp. 4005-4015
    • Kidd, D.1    Liu, Y.2    Cravatt, B.F.3
  • 18
    • 14844344010 scopus 로고    scopus 로고
    • The agony and ecstasy of 'OMIC' technologies in drug development
    • Bilello, J. A. (2005) The agony and ecstasy of 'OMIC' technologies in drug development. Curr. Mol. Med. 5, 39-52.
    • (2005) Curr. Mol. Med. , vol.5 , pp. 39-52
    • Bilello, J.A.1
  • 19
    • 33645995718 scopus 로고    scopus 로고
    • Independent regulation of MucD, an HrtA-like protease in Pseudomonas aeruginosa, and the role of it's proteolytic motif in alginate gene regulation
    • Wood, L. F., and Ohman, D. E. (2006) Independent regulation of MucD, an HrtA-like protease in Pseudomonas aeruginosa, and the role of it's proteolytic motif in alginate gene regulation. J. Bacteriol. 188, 3134-3137.
    • (2006) J. Bacteriol. , vol.188 , pp. 3134-3137
    • Wood, L.F.1    Ohman, D.E.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 24
    • 0021234203 scopus 로고
    • The irreversible inhibition of urokinase, kidney-cell plasminogen activator, plasmin and β-trypsin by 1-(N-6-amino-n-hexyl)carbamoylimidazole
    • Walker, B., and 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. (Pubitemid 14082312)
    • (1984) Biochemical Journal , vol.221 , Issue.1 , pp. 277-280
    • Walker, B.1    Elmore, D.T.2
  • 25
    • 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., and Tsou, C.-L. (1982) Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier. Biochemistry 21, 1028-1032.
    • (1982) Biochemistry , vol.21 , pp. 1028-1032
    • Tian, W.-X.1    Tsou, C.-L.2
  • 26
    • 0035788446 scopus 로고    scopus 로고
    • The roles of mucD and alginate in the virulence of Pseudomonas aeruginosa in plants, nematodes and mice
    • DOI 10.1046/j.1365-2958.2001.02580.x
    • Yorgey, P., Rahme, L. G., Tan, M.-W., and Ausubel, F. M. (2001) The roles of mucD and alginate in the virulence of Pseudomonas aeruginosa in plants, nematodes and mice. Mol. Microbiol. 41, 1063-1076. (Pubitemid 36124703)
    • (2001) Molecular Microbiology , vol.41 , Issue.5 , pp. 1063-1076
    • Yorgey, P.1    Rahme, L.G.2    Tan, M.-W.3    Ausubel, F.M.4
  • 27
    • 33646004871 scopus 로고    scopus 로고
    • Biochemical analysis of alginate biosynthesis protein AlgX from Pseudomonas aeruginosa: Purification of an AlgX-MucD (AlgY) protein complex
    • Gutsche, J., Remminghorst, U., and Rehm, B. H. A. (2005) Biochemical analysis of alginate biosynthesis protein AlgX from Pseudomonas aeruginosa: purification of an AlgX-MucD (AlgY) protein complex. Biochimie 88, 245-251.
    • (2005) Biochimie , vol.88 , pp. 245-251
    • Gutsche, J.1    Remminghorst, U.2    Rehm, B.H.A.3
  • 28
    • 0030034915 scopus 로고    scopus 로고
    • Two distinct loci affecting conversion to mucoidy in Pseudomonas aeruginosa in cystic fibrosis encode homologs of the serine protease HtrA
    • Boucher, J. C., Martinez-Salazar, J., Schurr, M. J., Mudd, M. H., Yu, H., and Deretic, V. (1996) Two distinct loci affecting conversion to mucoidy in Pseudomonas aeruginosa in cystic fibrosis encode homologs of the serine protease HtrA. J. Bacteriol. 178, 7369-7377. (Pubitemid 26030607)
    • (1996) Journal of Bacteriology , vol.178 , Issue.2 , pp. 511-523
    • Boucher, J.C.1    Martinez-Salazar, J.2    Schurr, M.J.3    Mudd, M.H.4    Yu, H.5    Deretic, V.6


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