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Volumn 14, Issue 1, 2003, Pages 110-118

Advances in quantitative proteomics via stable isotope tagging and mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

CARBON 13; ISOTOPE CODED AFFINITY TAG; LYSINE; MESSENGER RNA; REAGENT; STABLE ISOTOPE; UNCLASSIFIED DRUG;

EID: 0037307816     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(02)00018-6     Document Type: Review
Times cited : (247)

References (45)
  • 2
    • 0035241690 scopus 로고    scopus 로고
    • Mass spectrometry in proteomics
    • Aebersold R., Goodlett D.R. Mass spectrometry in proteomics. Chem. Rev. 101:2001;269-295.
    • (2001) Chem. Rev. , vol.101 , pp. 269-295
    • Aebersold, R.1    Goodlett, D.R.2
  • 3
    • 0035224918 scopus 로고    scopus 로고
    • Arrays for protein expression profiling: Towards a viable alternative to two-dimensional gel electrophoresis?
    • Jenkins R.E., Pennington S.R. Arrays for protein expression profiling: towards a viable alternative to two-dimensional gel electrophoresis? Proteomics. 1:2001;13-29.
    • (2001) Proteomics , vol.1 , pp. 13-29
    • Jenkins, R.E.1    Pennington, S.R.2
  • 4
  • 6
    • 0035805255 scopus 로고    scopus 로고
    • Integrated genomic and proteomic analyses of a systematically perturbed metabolic network
    • A pilot study demonstrating the Systems Biology approach that integrates quantitative data, at both the genomic and proteomic levels.
    • Ideker T., Thorsson V., Ranish J.A., Christmas R., Buhler J., Eng J.K., Bumgarner R., Goodlett D.R., Aebersold R., Hood L. Integrated genomic and proteomic analyses of a systematically perturbed metabolic network. Science. 292:2001;929-934 A pilot study demonstrating the Systems Biology approach that integrates quantitative data, at both the genomic and proteomic levels.
    • (2001) Science , vol.292 , pp. 929-934
    • Ideker, T.1    Thorsson, V.2    Ranish, J.A.3    Christmas, R.4    Buhler, J.5    Eng, J.K.6    Bumgarner, R.7    Goodlett, D.R.8    Aebersold, R.9    Hood, L.10
  • 7
    • 0036545614 scopus 로고    scopus 로고
    • Complementary profiling of gene expression at the transcriptome and proteome levels in Saccharomyces cerevisiae
    • Griffin T.J., Gygi S.P., Ideker T., Rist B., Eng J., Hood L., Aebersold R. Complementary profiling of gene expression at the transcriptome and proteome levels in Saccharomyces cerevisiae. Mol. Cell. Proteomics. 1:2002;323-333.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 323-333
    • Griffin, T.J.1    Gygi, S.P.2    Ideker, T.3    Rist, B.4    Eng, J.5    Hood, L.6    Aebersold, R.7
  • 8
    • 0037200031 scopus 로고    scopus 로고
    • A genomic and proteomic analysis of activation of the human neutrophil by lipopolysaccharide and its mediation by p38 mitogen-activated protein kinase
    • The authors demonstrate that the measurements of the cellular response to external perturbations at the mRNA and protein levels are complementary in mammalian cells.
    • Fessler M.B., Malcolm K.C., Duncan M.W., Worthen G.S. A genomic and proteomic analysis of activation of the human neutrophil by lipopolysaccharide and its mediation by p38 mitogen-activated protein kinase. J. Biol. Chem. 277:2002;31291-31302 The authors demonstrate that the measurements of the cellular response to external perturbations at the mRNA and protein levels are complementary in mammalian cells.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31291-31302
    • Fessler, M.B.1    Malcolm, K.C.2    Duncan, M.W.3    Worthen, G.S.4
  • 9
    • 0036792719 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of Myc oncoprotein function
    • Description of a novel quantitative proteomic approach to the analysis of Myc oncoprotein function, indicating the feasibility of quantitative whole-proteome analysis in mammalian cells.
    • Shiio Y., Donohoe S., Yi E.C., Goodlett D.R., Aebersold R., Eisenman R.N. Quantitative proteomic analysis of Myc oncoprotein function. EMBO J. 21:2002;5088-5096 Description of a novel quantitative proteomic approach to the analysis of Myc oncoprotein function, indicating the feasibility of quantitative whole-proteome analysis in mammalian cells.
    • (2002) EMBO J. , vol.21 , pp. 5088-5096
    • Shiio, Y.1    Donohoe, S.2    Yi, E.C.3    Goodlett, D.R.4    Aebersold, R.5    Eisenman, R.N.6
  • 10
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han D.K., Eng J., Zhou H., Aebersold R. Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat. Biotechnol. 19:2001;946-951.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 11
  • 13
    • 0036468952 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded affinity tags: Application to the enrichment and identification of low-abundance phosphoproteins
    • Goshe M.B., Veenstra T.D., Panisko E.A., Conrads T.P., Angell N.H., Smith R.D. Phosphoprotein isotope-coded affinity tags: application to the enrichment and identification of low-abundance phosphoproteins. Anal. Chem. 74:2002;607-616.
    • (2002) Anal. Chem. , vol.74 , pp. 607-616
    • Goshe, M.B.1    Veenstra, T.D.2    Panisko, E.A.3    Conrads, T.P.4    Angell, N.H.5    Smith, R.D.6
  • 14
    • 0036463388 scopus 로고    scopus 로고
    • Selective detection of membrane proteins without antibodies: A mass spectrometric version of the western blot
    • The paper has used the isotope-tagging technology for a novel approach. Rather than analysing global protein profiles, the technology has been used to monitor several important cell surface proteins in prostate cells.
    • Arnott D., Kishiyama A., Luis E.A., Ludlum S.G., Marsters J.C. Jr., Stults J.T. Selective detection of membrane proteins without antibodies: a mass spectrometric version of the western blot. Mol. Cell. Proteomics. 1:2002;148-156 The paper has used the isotope-tagging technology for a novel approach. Rather than analysing global protein profiles, the technology has been used to monitor several important cell surface proteins in prostate cells.
    • (2002) Mol. Cell. Proteomics. , vol.1 , pp. 148-156
    • Arnott, D.1    Kishiyama, A.2    Luis, E.A.3    Ludlum, S.G.4    Marsters J.C., Jr.5    Stults, J.T.6
  • 15
    • 0035499083 scopus 로고    scopus 로고
    • Fractionation of isotopically labeled peptides in quantitative proteomics
    • The authors have recognized potential resolution of isotopic forms of a peptide on reverse-phase chromatography and its resulting inconvenience in quantitative proteomics.
    • Zhang R., Sioma C.S., Wang S., Regnier F.E. Fractionation of isotopically labeled peptides in quantitative proteomics. Anal. Chem. 73:2001;5142-5149 The authors have recognized potential resolution of isotopic forms of a peptide on reverse-phase chromatography and its resulting inconvenience in quantitative proteomics.
    • (2001) Anal. Chem. , vol.73 , pp. 5142-5149
    • Zhang, R.1    Sioma, C.S.2    Wang, S.3    Regnier, F.E.4
  • 17
    • 0036789268 scopus 로고    scopus 로고
    • Acid-labile isotope-coded extractants: A class of reagents for quantitative mass spectrometric analysis of complex protein mixtures
    • •]. As a significant step toward the development of new quantitative proteomics reagents, the solid-phase approach facilitates fully robotized, high-throughput quantitative proteomic analysis.
    • •]. As a significant step toward the development of new quantitative proteomics reagents, the solid-phase approach facilitates fully robotized, high-throughput quantitative proteomic analysis.
    • (2002) Anal. Chem. , vol.74 , pp. 4969-4979
    • Qiu, Y.1    Sousa, E.A.2    Hewick, R.M.3    Wang, J.H.4
  • 19
    • 0034282457 scopus 로고    scopus 로고
    • Quantitation and facilitated de novo sequencing of proteins by isotopic N-terminal labeling of peptides with a fragmentation-directing moiety
    • Munchbach M., Quadroni M., Miotto G., James P. Quantitation and facilitated de novo sequencing of proteins by isotopic N-terminal labeling of peptides with a fragmentation-directing moiety. Anal. Chem. 72:2000;4047-4057.
    • (2000) Anal. Chem. , vol.72 , pp. 4047-4057
    • Munchbach, M.1    Quadroni, M.2    Miotto, G.3    James, P.4
  • 20
    • 0037040607 scopus 로고    scopus 로고
    • Global internal standard technology for comparative proteomics
    • Chakraborty A., Regnier F.E. Global internal standard technology for comparative proteomics. J. Chromatogr. A. 949:2002;173-184.
    • (2002) J. Chromatogr. A , vol.949 , pp. 173-184
    • Chakraborty, A.1    Regnier, F.E.2
  • 21
    • 0037040565 scopus 로고    scopus 로고
    • Quantitative proteomics strategy involving the selection of peptides containing both cysteine and histidine from tryptic digests of cell lysates
    • Wang S., Zhang X., Regnier F.E. Quantitative proteomics strategy involving the selection of peptides containing both cysteine and histidine from tryptic digests of cell lysates. J. Chromatogr. A. 949:2002;153-162.
    • (2002) J. Chromatogr. A , vol.949 , pp. 153-162
    • Wang, S.1    Zhang, X.2    Regnier, F.E.3
  • 22
    • 0037172367 scopus 로고    scopus 로고
    • Simplification of complex tryptic digests for capillary electrophoresis by affinity selection of histidine-containing peptides with immobilised metal ion affinity chromatography
    • Amini A., Chakraborty A., Regnier F.E. Simplification of complex tryptic digests for capillary electrophoresis by affinity selection of histidine-containing peptides with immobilised metal ion affinity chromatography. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 772:2002;35-44.
    • (2002) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.772 , pp. 35-44
    • Amini, A.1    Chakraborty, A.2    Regnier, F.E.3
  • 23
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou H., Watts J.D., Aebersold R. A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 19:2001;375-378.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 24
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda Y., Nagasu T., Chait B.T. Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 19:2001;379-382.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 26
    • 0035836061 scopus 로고    scopus 로고
    • Proteomics of glycoproteins based on affinity selection of glycopeptides from tryptic digests
    • Geng M., Zhang X., Bina M., Regnier F. Proteomics of glycoproteins based on affinity selection of glycopeptides from tryptic digests. J. Chromatogr. B. Biomed. Sci. Appl. 752:2001;293-306.
    • (2001) J. Chromatogr. B. Biomed. Sci. Appl. , vol.752 , pp. 293-306
    • Geng, M.1    Zhang, X.2    Bina, M.3    Regnier, F.4
  • 27
    • 0035384687 scopus 로고    scopus 로고
    • 18O labeling for comparative proteomics: Model studies with two serotypes of adenovirus
    • 18O labeling for comparative proteomics: model studies with two serotypes of adenovirus Anal. Chem. 73:2001;2836-2842.
    • (2001) Anal. Chem. , vol.73 , pp. 2836-2842
    • Yao, X.1    Freas, A.2    Ramirez, J.3    Demirev, P.A.4    Fenselau, C.5
  • 30
    • 0033535961 scopus 로고    scopus 로고
    • Accurate quantitation of protein expression and site-specific phosphorylation
    • Oda Y., Huang K., Cross F.R., Cowburn D., Chait B.T. Accurate quantitation of protein expression and site-specific phosphorylation. Proc. Natl. Acad. Sci. USA. 96:1999;6591-6596.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6591-6596
    • Oda, Y.1    Huang, K.2    Cross, F.R.3    Cowburn, D.4    Chait, B.T.5
  • 31
    • 0036535357 scopus 로고    scopus 로고
    • Analysis of quantitative proteomic data generated via multidimensional protein identification technology
    • Washburn M.P., Ulaszek R., Deciu C., Schieltz D.M., Yates J.R. III Analysis of quantitative proteomic data generated via multidimensional protein identification technology. Anal. Chem. 74:2002;1650-1657.
    • (2002) Anal. Chem. , vol.74 , pp. 1650-1657
    • Washburn, M.P.1    Ulaszek, R.2    Deciu, C.3    Schieltz, D.M.4    Yates J.R. III5
  • 32
    • 0032578463 scopus 로고    scopus 로고
    • Counting individual sulfur atoms in a protein by ultrahigh-resolution Fourier transform ion cyclotron resonance mass spectrometry: Experimental resolution of isotopic fine structure in proteins
    • Shi S.D., Hendrickson C.L., Marshall A.G. Counting individual sulfur atoms in a protein by ultrahigh-resolution Fourier transform ion cyclotron resonance mass spectrometry: experimental resolution of isotopic fine structure in proteins. Proc. Natl. Acad. Sci. USA. 95:1998;11532-11537.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11532-11537
    • Shi, S.D.1    Hendrickson, C.L.2    Marshall, A.G.3
  • 33
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Stable isotope labeling was applied to mammalian cells by in vivo incorporation of specific amino acids during cell culture.
    • Ong S.E., Blagoev B., Kratchmarova I., Kristensen D.B., Steen H., Pandey A., Mann M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics. 1:2002;376-386 Stable isotope labeling was applied to mammalian cells by in vivo incorporation of specific amino acids during cell culture.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 34
    • 0036164157 scopus 로고    scopus 로고
    • Selective incorporation of isotopically labeled amino acids for identification of intact proteins on a proteome-wide level
    • Martinovic S., Veenstra T.D., Anderson G.A., Pasa-Tolic L., Smith R.D. Selective incorporation of isotopically labeled amino acids for identification of intact proteins on a proteome-wide level. J. Mass Spectrom. 37:2002;99-107.
    • (2002) J. Mass Spectrom. , vol.37 , pp. 99-107
    • Martinovic, S.1    Veenstra, T.D.2    Anderson, G.A.3    Pasa-Tolic, L.4    Smith, R.D.5
  • 35
    • 0036428393 scopus 로고    scopus 로고
    • Amino acid residue specific stable isotope labeling for quantitative proteomics
    • Zhu H., Pan S., Gu S., Bradbury E.M., Chen X. Amino acid residue specific stable isotope labeling for quantitative proteomics. Rapid. Commun. Mass Spectrom. 16:2002;2115-2123.
    • (2002) Rapid. Commun. Mass Spectrom. , vol.16 , pp. 2115-2123
    • Zhu, H.1    Pan, S.2    Gu, S.3    Bradbury, E.M.4    Chen, X.5
  • 36
    • 0036535518 scopus 로고    scopus 로고
    • Residue-specific mass signatures for the efficient detection of protein modifications by mass spectrometry
    • Zhu H., Hunter T.C., Pan S., Yau P.M., Bradbury E.M., Chen X. Residue-specific mass signatures for the efficient detection of protein modifications by mass spectrometry. Anal. Chem. 74:2002;1687-1694.
    • (2002) Anal. Chem. , vol.74 , pp. 1687-1694
    • Zhu, H.1    Hunter, T.C.2    Pan, S.3    Yau, P.M.4    Bradbury, E.M.5    Chen, X.6
  • 37
    • 0036171359 scopus 로고    scopus 로고
    • De novo peptide sequencing and quantitative profiling of complex protein mixtures using mass-coded abundance tagging
    • Cagney G., Emili A. De novo peptide sequencing and quantitative profiling of complex protein mixtures using mass-coded abundance tagging. Nat. Biotechnol. 20:2002;163-170.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 163-170
    • Cagney, G.1    Emili, A.2
  • 38
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A., Nesvizhskii A.I., Kolker E., Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 74:2002;5383-5392.
    • (2002) Anal. Chem. , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 39
    • 0035563654 scopus 로고    scopus 로고
    • Toward a high-throughput approach to quantitative proteomic analysis: Expression-dependent protein identification by mass spectrometry
    • Griffin T.J., Han D.K., Gygi S.P., Rist B., Lee H., Aebersold R., Parker K.C. Toward a high-throughput approach to quantitative proteomic analysis: expression-dependent protein identification by mass spectrometry. J. Am. Soc. Mass Spectrom. 12:2001;1238-1246.
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 1238-1246
    • Griffin, T.J.1    Han, D.K.2    Gygi, S.P.3    Rist, B.4    Lee, H.5    Aebersold, R.6    Parker, K.C.7
  • 41
    • 0034132537 scopus 로고    scopus 로고
    • The characteristics of peptide collision-induced dissociation using a high-performance MALDI-TOF/TOF tandem mass spectrometer
    • Medzihradszky K.F., Campbell J.M., Baldwin M.A., Falick A.M., Juhasz P., Vestal M.L., Burlingame A.L. The characteristics of peptide collision-induced dissociation using a high-performance MALDI-TOF/TOF tandem mass spectrometer. Anal. Chem. 72:2000;552-558.
    • (2000) Anal. Chem. , vol.72 , pp. 552-558
    • Medzihradszky, K.F.1    Campbell, J.M.2    Baldwin, M.A.3    Falick, A.M.4    Juhasz, P.5    Vestal, M.L.6    Burlingame, A.L.7
  • 42
    • 0036712835 scopus 로고    scopus 로고
    • Development of a multiplexed microcapillary liquid chromatography system for high-throughput proteome analysis
    • Lee H., Griffin T.J., Gygi S.P., Rist B., Aebersold R. Development of a multiplexed microcapillary liquid chromatography system for high-throughput proteome analysis. Anal. Chem. 74:2002;4353-4360.
    • (2002) Anal. Chem. , vol.74 , pp. 4353-4360
    • Lee, H.1    Griffin, T.J.2    Gygi, S.P.3    Rist, B.4    Aebersold, R.5
  • 43
    • 0035499655 scopus 로고    scopus 로고
    • Automatic identification of proteins with a MALDI-quadrupole ion trap mass spectrometer
    • Krutchinsky A.N., Kalkum M., Chait B.T. Automatic identification of proteins with a MALDI-quadrupole ion trap mass spectrometer. Anal. Chem. 73:2001;5066-5077.
    • (2001) Anal. Chem. , vol.73 , pp. 5066-5077
    • Krutchinsky, A.N.1    Kalkum, M.2    Chait, B.T.3
  • 44
    • 0036083630 scopus 로고    scopus 로고
    • Cutting-edge technology. II. Proteomics: Core technologies and applications in physiology
    • Witzmann F.A., Li J. Cutting-edge technology. II. Proteomics: core technologies and applications in physiology. Am. J. Physiol. Gastrointest. Liver Physiol. 282:2002;G735-G741.
    • (2002) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.282
    • Witzmann, F.A.1    Li, J.2
  • 45
    • 0036683062 scopus 로고    scopus 로고
    • Proteomics approaches in drug discovery
    • Figeys D. Proteomics approaches in drug discovery. Anal. Chem. 74:2002;412A-419A.
    • (2002) Anal. Chem. , vol.74
    • Figeys, D.1


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