메뉴 건너뛰기




Volumn 441, Issue 2, 2013, Pages 123-132

An aptamer-based trypsin reactor for on-line protein digestion with electrospray ionization tandem mass spectrometry

Author keywords

Aptamer; Digestion; Mass spectrometry identification; Protein; Trypsin

Indexed keywords

DISSOCIATION; DNA; ENZYME IMMOBILIZATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PROTEINS; SILICA; SLUDGE DIGESTION;

EID: 84884962201     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2013.06.012     Document Type: Article
Times cited : (17)

References (34)
  • 1
    • 0037434980 scopus 로고    scopus 로고
    • From genomics to proteomics
    • DOI 10.1038/nature01510
    • M. Tyers, M. Mann, From genomics to proteomics, Nature 422 (2003) 193-197. (Pubitemid 36362756)
    • (2003) Nature , vol.422 , Issue.6928 , pp. 193-197
    • Tyers, M.1    Mann, M.2
  • 2
    • 33749615256 scopus 로고    scopus 로고
    • Mass spectrometry: Bottom-up or top-down?
    • DOI 10.1126/science.1133987
    • B.T. Chait, Mass spectrometry: bottom-up or top-down?, Science 314 (2006) 65-66 (Pubitemid 44547738)
    • (2006) Science , vol.314 , Issue.5796 , pp. 65-66
    • Chait, B.T.1
  • 4
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • J.R. Yates, C.I. Ruse, A. Nakorchevsky, Proteomics by mass spectrometry: approaches, advances, and applications, Annu. Rev. Biomed. Eng. 11 (2009) 49-79.
    • (2009) Annu. Rev. Biomed. Eng. , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 6
    • 10944250656 scopus 로고    scopus 로고
    • Immobilized microfluidic enzymatic reactors
    • DOI 10.1002/elps.200406096
    • J. Krenkova, F. Foret, Immobilized microfluidic enzymatic reactors, Electrophoresis 25 (2004) 3550-3563. (Pubitemid 40012112)
    • (2004) Electrophoresis , vol.25 , Issue.21-22 , pp. 3550-3563
    • Krenkova, J.1    Foret, F.2
  • 7
    • 13444302620 scopus 로고    scopus 로고
    • Immobilized trypsin systems coupled on-line to separation methods: Recent developments and analytical applications
    • DOI 10.1002/jssc.200401941
    • G. Massolini, E. Calleri, Immobilized trypsin systems coupled on-line to separation methods: recent developments and analytical applications, J. Sep. Sci. 28 (2005) 7-21. (Pubitemid 40214460)
    • (2005) Journal of Separation Science , vol.28 , Issue.1 , pp. 7-21
    • Massolini, G.1    Calleri, E.2
  • 8
    • 0037355581 scopus 로고    scopus 로고
    • Membrane-based nanoscale proteolytic reactor enabling protein digestion, peptide separation, and protein identification using mass spectrometry
    • DOI 10.1021/ac025768b
    • J.W. Cooper, J. Chen, Y. Li, C.S. Lee, Membrane-based nanoscale proteolytic reactor enabling protein digestion, peptide separation, and protein identification using mass spectrometry, Anal. Chem. 75 (2003) 1067-1074. (Pubitemid 36402634)
    • (2003) Analytical Chemistry , vol.75 , Issue.5 , pp. 1067-1074
    • Cooper, J.W.1    Chen, J.2    Li, Y.3    Lee, C.S.4
  • 9
    • 61449087368 scopus 로고    scopus 로고
    • Trypsin immobilization on an ethylenediamine-based monolithic minidisk for rapid on-line peptide mass fingerprinting studies
    • R. Nicoli, S. Rudaz, C. Stella, J.L. Veuthey, Trypsin immobilization on an ethylenediamine-based monolithic minidisk for rapid on-line peptide mass fingerprinting studies, J. Chromatogr. A 1216 (2009) 2695-2699.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 2695-2699
    • Nicoli, R.1    Rudaz, S.2    Stella, C.3    Veuthey, J.L.4
  • 10
    • 65449162340 scopus 로고    scopus 로고
    • Less common applications of monoliths: IV. Recent developments in immobilized enzyme reactors for proteomics and biotechnology
    • J. Krenkova, F. Svec, Less common applications of monoliths: IV. Recent developments in immobilized enzyme reactors for proteomics and biotechnology, J. Sep. Sci. 32 (2009) 706-718.
    • (2009) J. Sep. Sci. , vol.32 , pp. 706-718
    • Krenkova, J.1    Svec, F.2
  • 11
    • 34547209337 scopus 로고    scopus 로고
    • Enzyme immobilization: The quest for optimum performance
    • R.A. Sheldon, Enzyme immobilization: the quest for optimum performance, Adv. Synth. Catal. 349 (2007) 1289-1307.
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1289-1307
    • Sheldon, R.A.1
  • 12
    • 37049015378 scopus 로고    scopus 로고
    • Sol-gels and cross-linked aggregates of lipase PS from Burkholderia cepacia and their application in dry organic solvents
    • DOI 10.1016/j.molcatb.2007.09.004, PII S1381117707001749, Contriburions by COST Action D25: Applied Biocatalysis. Stereoselective and Environmentally Friendly Reactions Catalysed by Enzymes
    • P. Hara, U. Hanefeld, L.T. Kanerva, Sol-gels and cross-linked aggregates of lipase PS from Burkholderia cepacia and their application in dry organic solvents, J. Mol. Catal. B 50 (2008) 80-86. (Pubitemid 350245630)
    • (2008) Journal of Molecular Catalysis B: Enzymatic , vol.50 , Issue.2-4 , pp. 80-86
    • Hara, P.1    Hanefeld, U.2    Kanerva, L.T.3
  • 13
    • 29244470287 scopus 로고    scopus 로고
    • Nanovolume kinase inhibition assay using a sol-gel-derived multicomponent microarray
    • DOI 10.1021/ac051405a
    • N. Rupcich, J.R.A. Green, J.D. Brennan, Nanovolume kinase inhibition assay using a sol-gel-derived multicomponent microarray, Anal. Chem. 77 (2005) 8013-8019. (Pubitemid 41831987)
    • (2005) Analytical Chemistry , vol.77 , Issue.24 , pp. 8013-8019
    • Rupcich, N.1    Green, J.R.A.2    Brennan, J.D.3
  • 14
    • 84862881107 scopus 로고    scopus 로고
    • Nanoreactors by programmed enzyme encapsulation inside the capsid of the bacteriophage P22
    • D.P. Patterson, P.E. Prevelige, T. Douglas, Nanoreactors by programmed enzyme encapsulation inside the capsid of the bacteriophage P22, ACS Nano 6 (2012) 5000-5009.
    • (2012) ACS Nano , vol.6 , pp. 5000-5009
    • Patterson, D.P.1    Prevelige, P.E.2    Douglas, T.3
  • 15
    • 0025074907 scopus 로고
    • In vitro selection of RNA molecules that bind specific ligands
    • A.D. Ellington, J.W. Szostak, In vitro selection of RNA molecules that bind specific ligands, Nature 346 (1990) 818-822.
    • (1990) Nature , vol.346 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.W.2
  • 16
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • C. Tuerk, L. Gold, Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase, Science 249 (1990) 505-510.
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 17
    • 14544295783 scopus 로고    scopus 로고
    • Aptamers: An emerging class of therapeutics
    • DOI 10.1146/annurev.med.56.062904.144915
    • S.M. Nimjee, C.P. Rusconi, B.A. Sullenger, Aptamers: an emerging class of therapeutics, Annu. Rev. Med. 56 (2005) 555-583. (Pubitemid 40299797)
    • (2005) Annual Review of Medicine , vol.56 , pp. 555-583
    • Nimjee, S.M.1    Rusconi, C.P.2    Sullenger, B.A.3
  • 19
    • 68249092118 scopus 로고    scopus 로고
    • Aptamers as inhibitors of target proteins
    • S. Missailidis, A. Hardy, Aptamers as inhibitors of target proteins, Expert Opin. Ther. Pat. 19 (2009) 1073-1082.
    • (2009) Expert Opin. Ther. Pat. , vol.19 , pp. 1073-1082
    • Missailidis, S.1    Hardy, A.2
  • 22
    • 34347260679 scopus 로고    scopus 로고
    • Proteomics in 2005/2006: Developments, applications and challenges
    • DOI 10.1021/ac070741j
    • J.C. Smith, J.P. Lambert, F. Elisma, D. Figeys, Proteomics in 2005/2006: developments, applications, and challenges, Anal. Chem. 79 (2007) 4325-4343. (Pubitemid 46999548)
    • (2007) Analytical Chemistry , vol.79 , Issue.12 , pp. 4325-4343
    • Smith, J.C.1    Lambert, J.-P.2    Elisma, F.3    Figeys, D.4
  • 23
    • 54249140142 scopus 로고    scopus 로고
    • RNA computing in a living cell
    • E. Shapiro, B. Gil, RNA computing in a living cell, Science 322 (2008) 387-388.
    • (2008) Science , vol.322 , pp. 387-388
    • Shapiro, E.1    Gil, B.2
  • 24
    • 79959247146 scopus 로고    scopus 로고
    • Aptamer in bioanalytical applications
    • A.B. Iliuk, L. Hu, W.A. Tao, Aptamer in bioanalytical applications, Anal. Chem. 83 (2011) 4440-4452.
    • (2011) Anal. Chem. , vol.83 , pp. 4440-4452
    • Iliuk, A.B.1    Hu, L.2    Tao, W.A.3
  • 25
    • 34548686312 scopus 로고    scopus 로고
    • Semi-automated selection of DNA aptamers using magnetic particle handling
    • A. Wochner, B. Cech, M. Menger, V.A. Erdmann, J. Glokler, Semi-automated selection of DNA aptamers using magnetic particle handling, BioTechniques 43 (2007) 344-348.
    • (2007) BioTechniques , vol.43 , pp. 344-348
    • Wochner, A.1    Cech, B.2    Menger, M.3    Erdmann, V.A.4    Glokler, J.5
  • 27
    • 33646909444 scopus 로고    scopus 로고
    • Thermodynamic characterization of an engineered tetracycline-binding riboswitch
    • DOI 10.1093/nar/gkl347
    • M. Muller, J.E. Weigand, O. Weichenrieder, B. Suess, Thermodynamic characterization of an engineered tetracycline-binding riboswitch, Nucleic Acids Res. 34 (2006) 2607-2617. (Pubitemid 43985625)
    • (2006) Nucleic Acids Research , vol.34 , Issue.9 , pp. 2607-2617
    • Muller, M.1    Weigand, J.E.2    Weichenrieder, O.3    Suess, B.4
  • 28
    • 38849186073 scopus 로고    scopus 로고
    • SsDNA aptamers that selectively bind oxytetracycline
    • DOI 10.1016/j.bmc.2007.10.073, PII S0968089607009406
    • J.H. Niazi, S.J. Lee, Y.S. Kim, M.B. Gu, SsDNA aptamers that selectively bind oxytetracycline, Bioorg. Med. Chem. 16 (2008) 1254-1261. (Pubitemid 351191776)
    • (2008) Bioorganic and Medicinal Chemistry , vol.16 , Issue.3 , pp. 1254-1261
    • Niazi, J.H.1    Lee, S.J.2    Kim, Y.S.3    Gu, M.B.4
  • 29
    • 33646048032 scopus 로고    scopus 로고
    • The thrombin binding aptamer GGTTGGTGTGGTTGG forms a bimolecular guanine tetraplex
    • M. Fialova, J. Kypr, M. Vorlickova, The thrombin binding aptamer GGTTGGTGTGGTTGG forms a bimolecular guanine tetraplex, Biochem. Biophys. Res. Commun. 344 (2006) 50-54.
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 50-54
    • Fialova, M.1    Kypr, J.2    Vorlickova, M.3
  • 30
    • 0028965943 scopus 로고
    • A DNA aptamer that binds adenosine and ATP
    • D.E. Huizenga, J.W. Szostak, A DNA aptamer that binds adenosine and ATP, Biochemistry 34 (1995) 656-665.
    • (1995) Biochemistry , vol.34 , pp. 656-665
    • Huizenga, D.E.1    Szostak, J.W.2
  • 31
    • 0034846294 scopus 로고    scopus 로고
    • In vitro selection of DNA aptamers that bind L-tyrosinamide
    • DOI 10.1016/S0968-0896(01)00054-2, PII S0968089601000542
    • E. Vianini, M. Palumbo, B. Gatto, In vitro selection of DNA aptamers that bind ltyrosinamide, Bioorg. Med. Chem. 9 (2001) 2543-2548. (Pubitemid 32824156)
    • (2001) Bioorganic and Medicinal Chemistry , vol.9 , Issue.10 , pp. 2543-2548
    • Vianini, E.1    Palumbo, M.2    Gatto, B.3
  • 32
    • 84872720270 scopus 로고    scopus 로고
    • An enzyme reactor based on aptamer modified microfluidic chip for protein analysis
    • P. Xiao, D. Li, Y. Man, L. Geng, X. Lv, Y. Deng, An enzyme reactor based on aptamer modified microfluidic chip for protein analysis, Chin. J. Chromatogr. 30 (2012) 1127-1132.
    • (2012) Chin. J. Chromatogr. , vol.30 , pp. 1127-1132
    • Xiao, P.1    Li, D.2    Man, Y.3    Geng, L.4    Lv, X.5    Deng, Y.6
  • 33
    • 76849103926 scopus 로고    scopus 로고
    • A capillary monolithic trypsin reactor for efficient protein digestion in online and offline coupling to ESI and MALDI mass spectrometry
    • J. Spross, A. Sinz, A capillary monolithic trypsin reactor for efficient protein digestion in online and offline coupling to ESI and MALDI mass spectrometry, Anal. Chem. 82 (2010) 1434-1443.
    • (2010) Anal. Chem. , vol.82 , pp. 1434-1443
    • Spross, J.1    Sinz, A.2
  • 34
    • 79959259512 scopus 로고    scopus 로고
    • Analyzing nanomaterial bioconjugates: A review of current and emerging purification and characterization techniques
    • K.E. Sapsford, K.M. Tyner, B.J. Dair, J.R. Deschamps, I.L. Medintz, Analyzing nanomaterial bioconjugates: a review of current and emerging purification and characterization techniques, Anal. Chem. 83 (2011) 4453-4488.
    • (2011) Anal. Chem. , vol.83 , pp. 4453-4488
    • Sapsford, K.E.1    Tyner, K.M.2    Dair, B.J.3    Deschamps, J.R.4    Medintz, I.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.