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Volumn 6, Issue 2, 2011, Pages 147-157

Use of stable isotope labeling by amino acids in cell culture as a spike-in standard in quantitative proteomics

Author keywords

[No Author keywords available]

Indexed keywords

PROTEOME;

EID: 79551663189     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2010.192     Document Type: Article
Times cited : (234)

References (44)
  • 1
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D.A., Washburn, M.P. & Yates, J.R. III. An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 73, 5683-5690 (2001).
    • (2001) Anal. Chem. , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 2
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R. & Mann, M. Mass spectrometry-based proteomics. Nature 422, 198-207 (2003).
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 3
    • 4444335470 scopus 로고    scopus 로고
    • The ABCs and XYZs of peptide sequencing
    • Steen, H. & Mann, M. The ABCs (and XYZs) of peptide sequencing. Nat. Rev. Mol. Cell. Biol. 5, 699-711 (2004).
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 4
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S.E. & Mann, M. Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 1, 252-262 (2005).
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 5
    • 48849097164 scopus 로고    scopus 로고
    • Quantitative proteomics as a new piece of the systems biology puzzle
    • Bachi, A. & Bonaldi, T. Quantitative proteomics as a new piece of the systems biology puzzle. J. Proteomics 71, 357-367 (2008).
    • (2008) J. Proteomics , vol.71 , pp. 357-367
    • Bachi, A.1    Bonaldi, T.2
  • 7
    • 15944377809 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway
    • Gruhler, A. et al. Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway. Mol. Cell. Proteomics 4, 310-327 (2005).
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 310-327
    • Gruhler, A.1
  • 8
    • 33846706581 scopus 로고    scopus 로고
    • TOPP-the OpenMS proteomics pipeline
    • Kohlbacher, O. et al. TOPP-the OpenMS proteomics pipeline. Bioinformatics 23, e191-e197 (2007).
    • (2007) Bioinformatics , vol.23
    • Kohlbacher, O.1
  • 9
    • 35348965139 scopus 로고    scopus 로고
    • SuperHirn-a novel tool for high resolution LC-MS-based peptide/protein profiling
    • Mueller, L.N. et al. SuperHirn-a novel tool for high resolution LC-MS-based peptide/protein profiling. Proteomics 7, 3470-3480 (2007).
    • (2007) Proteomics , vol.7 , pp. 3470-3480
    • Mueller, L.N.1
  • 10
    • 76949097340 scopus 로고    scopus 로고
    • Quantitative proteomics reveals subset-specific viral recognition in dendritic cells
    • Luber, C.A. et al. Quantitative proteomics reveals subset-specific viral recognition in dendritic cells. Immunity 32, 279-289 (2010).
    • (2010) Immunity , vol.32 , pp. 279-289
    • Luber, C.A.1
  • 11
    • 33750594230 scopus 로고    scopus 로고
    • Chemistry meets proteomics: The use of chemical tagging reactions for MS-based proteomics
    • Leitner, A. & Lindner, W. Chemistry meets proteomics: the use of chemical tagging reactions for MS-based proteomics. Proteomics 6, 5418-5434 (2006).
    • (2006) Proteomics , vol.6 , pp. 5418-5434
    • Leitner, A.1    Lindner, W.2
  • 12
    • 16344389629 scopus 로고    scopus 로고
    • Metabolic labeling of proteins for proteomics
    • Beynon, R.J. & Pratt, J.M. Metabolic labeling of proteins for proteomics. Mol. Cell. Proteomics 4, 857-872 (2005).
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 857-872
    • Beynon, R.J.1    Pratt, J.M.2
  • 13
    • 76649083593 scopus 로고    scopus 로고
    • Quantitative proteomics by metabolic labeling of model organisms
    • Gouw, J.W., Krijgsveld, J. & Heck, A.J. Quantitative proteomics by metabolic labeling of model organisms. Mol. Cell. Proteomics 9, 11-24 (2010).
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 11-24
    • Gouw, J.W.1    Krijgsveld, J.2    Heck, A.J.3
  • 14
    • 0033535961 scopus 로고    scopus 로고
    • Accurate quantitation of protein expression and site-specific phosphorylation
    • USA
    • 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, 6591-6596 (1999).
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 6591-6596
    • Oda, Y.1    Huang, K.2    Cross, F.R.3    Cowburn, D.4    Chait, B.T.5
  • 15
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture silac as a simple and accurate approach to expression proteomics
    • Ong, S.E. et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386 (2002).
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1
  • 16
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using silac
    • Mann, M. Functional and quantitative proteomics using SILAC. Nat. Rev. Mol. Cell. Biol. 7, 952-958 (2006).
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , pp. 952-958
    • Mann, M.1
  • 17
    • 44449162195 scopus 로고    scopus 로고
    • Absolute silac for accurate quantitation of proteins in complex mixtures down to the attomole level
    • Hanke, S., Besir, H., Oesterhelt, D. & Mann, M. Absolute SILAC for accurate quantitation of proteins in complex mixtures down to the attomole level. J. Proteome Res. 7, 1118-1130 (2008).
    • (2008) J. Proteome Res. , vol.7 , pp. 1118-1130
    • Hanke, S.1    Besir, H.2    Oesterhelt, D.3    Mann, M.4
  • 18
    • 77954371891 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture silac applied to quantitative proteomics of bacillus subtilis
    • Soufi, B. et al. Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis. J. Proteome Res. 9, 3638-3646 (2010).
    • (2010) J. Proteome Res. , vol.9 , pp. 3638-3646
    • Soufi, B.1
  • 19
    • 33745591083 scopus 로고    scopus 로고
    • Status of complete proteome analysis by mass spectrometry: Silac labeled yeast as a model system
    • de Godoy, L.M. et al. Status of complete proteome analysis by mass spectrometry: SILAC labeled yeast as a model system. Genome Biol. 7, R50 (2006).
    • (2006) Genome Biol. , vol.7
    • De Godoy, L.M.1
  • 20
    • 77958018495 scopus 로고    scopus 로고
    • The silac fly allows for accurate protein quantification in vivo
    • Sury, M.D., Chen, J.X. & Selbach, M. The SILAC fly allows for accurate protein quantification in vivo. Mol. Cell. Proteomics 9, 2173-2183 (2010).
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2173-2183
    • Sury, M.D.1    Chen, J.X.2    Selbach, M.3
  • 21
    • 47549099572 scopus 로고    scopus 로고
    • Silac mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function
    • Kruger, M. et al. SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function. Cell 134, 353-364 (2008).
    • (2008) Cell , vol.134 , pp. 353-364
    • Kruger, M.1
  • 22
    • 77952226764 scopus 로고    scopus 로고
    • Super-silac mix for quantitative proteomics of human tumor tissue
    • Geiger, T., Cox, J., Ostasiewicz, P., Wisniewski, J.R. & Mann, M. Super-SILAC mix for quantitative proteomics of human tumor tissue. Nat. Methods 7, 383-385 (2010).
    • (2010) Nat. Methods , vol.7 , pp. 383-385
    • Geiger, T.1    Cox, J.2    Ostasiewicz, P.3    Wisniewski, J.R.4    Mann, M.5
  • 23
    • 22844436250 scopus 로고    scopus 로고
    • Quantitative mouse brain proteomics using culture-derived isotope tags as internal standards
    • Ishihama, Y. et al. Quantitative mouse brain proteomics using culture-derived isotope tags as internal standards. Nat. Biotechnol. 23, 617-621 (2005).
    • (2005) Nat. Biotechnol. , vol.23 , pp. 617-621
    • Ishihama, Y.1
  • 24
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture silac
    • Ong, S.E. & Mann, M. A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat. Protoc. 1, 2650-2660 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 25
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • USA
    • Gerber, S.A., Rush, J., Stemman, O., Kirschner, M.W. & Gygi, S.P. Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc. Natl. Acad. Sci. USA 100, 6940-6945 (2003).
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 26
    • 23144442824 scopus 로고    scopus 로고
    • Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides
    • Beynon, R.J., Doherty, M.K., Pratt, J.M. & Gaskell, S.J. Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides. Nat. Methods 2, 587-589 (2005).
    • (2005) Nat. Methods , vol.2 , pp. 587-589
    • Beynon, R.J.1    Doherty, M.K.2    Pratt, J.M.3    Gaskell, S.J.4
  • 27
    • 33847179916 scopus 로고    scopus 로고
    • Multiplexed absolute quantification for proteomics using concatenated signature peptides encoded by qconcat genes
    • Pratt, J.M. et al. Multiplexed absolute quantification for proteomics using concatenated signature peptides encoded by QconCAT genes. Nat. Protoc. 1, 1029-1043 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 1029-1043
    • Pratt, J.M.1
  • 28
    • 66749190541 scopus 로고    scopus 로고
    • Flexiquant: A novel tool for the absolute quantification of proteins and the simultaneous identification and quantification of potentially modified peptides
    • Singh, S., Springer, M., Steen, J., Kirschner, M.W. & Steen, H. FLEXIQuant: a novel tool for the absolute quantification of proteins, and the simultaneous identification and quantification of potentially modified peptides. J. Proteome Res. 8, 2201-2210 (2009).
    • (2009) J. Proteome Res. , vol.8 , pp. 2201-2210
    • Singh, S.1    Springer, M.2    Steen, J.3    Kirschner, M.W.4    Steen, H.5
  • 29
    • 38349037650 scopus 로고    scopus 로고
    • Isotope-labeled protein standards: Toward absolute quantitative proteomics
    • Brun, V. et al. Isotope-labeled protein standards: toward absolute quantitative proteomics. Mol. Cell. Proteomics 6, 2139-2149 (2007).
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2139-2149
    • Brun, V.1
  • 30
    • 55249096894 scopus 로고    scopus 로고
    • Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast
    • de Godoy, L.M. et al. Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast. Nature 455, 1251-1254 (2008).
    • (2008) Nature , vol.455 , pp. 1251-1254
    • De Godoy, L.M.1
  • 31
    • 77954695928 scopus 로고    scopus 로고
    • A genetic engineering solution to the arginine conversion problem in stable isotope labeling by amino acids in cell culture silac
    • Bicho, C.C., de Lima Alves, F., Chen, Z.A., Rappsilber, J. & Sawin, K.E. A genetic engineering solution to the Arginine Conversion Problem in stable isotope labeling by amino acids in cell culture (SILAC). Mol. Cell. Proteomics 9, 1567-1577 (2010).
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1567-1577
    • Bicho, C.C.1    De Lima Alves, F.2    Chen, Z.A.3    Rappsilber, J.4    Sawin, K.E.5
  • 32
    • 79953231670 scopus 로고    scopus 로고
    • Accurate quantification of more than 4000 mouse tissue proteins reveals minimal proteome changes during aging
    • published online 10.1074/mcp.M110.004523 3 November
    • Walther, D.M. & Mann, M. Accurate quantification of more than 4,000 mouse tissue proteins reveals minimal proteome changes during aging. Mol. Cell. Proteomics 9 published online, doi: 10.1074/mcp.M110.004523 (3 November 2010).
    • (2010) Mol. Cell. Proteomics , vol.9
    • Walther, D.M.1    Mann, M.2
  • 33
    • 33750319346 scopus 로고    scopus 로고
    • Orbitrap mass analyzer-overview and applications in proteomics
    • Scigelova, M. & Makarov, A. Orbitrap mass analyzer-overview and applications in proteomics. Proteomics 6 (Suppl 2): 16-21 (2006).
    • (2006) Proteomics , vol.6 , Issue.2 , pp. 16-21
    • Scigelova, M.1    Makarov, A.2
  • 34
    • 33645654439 scopus 로고    scopus 로고
    • Performance evaluation of a hybrid linear ion trap/orbitrap mass spectrometer
    • Makarov, A. et al. Performance evaluation of a hybrid linear ion trap/orbitrap mass spectrometer. Anal. Chem. 78, 2113-2120 (2006).
    • (2006) Anal. Chem. , vol.78 , pp. 2113-2120
    • Makarov, A.1
  • 35
    • 75149144996 scopus 로고    scopus 로고
    • A dual pressure linear ion trap orbitrap instrument with very high sequencing speed
    • Olsen, J.V. et al. A dual pressure linear ion trap Orbitrap instrument with very high sequencing speed. Mol. Cell. Proteomics 8, 2759-2769 (2009).
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2759-2769
    • Olsen, J.V.1
  • 36
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J.V. & Mann, M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856-2860 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 37
    • 75149180460 scopus 로고    scopus 로고
    • Unbiased quantitation of escherichia coli membrane proteome using phase transfer surfactants
    • Masuda, T., Saito, N., Tomita, M. & Ishihama, Y. Unbiased quantitation of Escherichia coli membrane proteome using phase transfer surfactants. Mol. Cell. Proteomics 8, 2770-2777 (2009).
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2770-2777
    • Masuda, T.1    Saito, N.2    Tomita, M.3    Ishihama, Y.4
  • 38
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J. & Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372 (2008).
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 39
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the maxquant computational platform for silac-based quantitative proteomics
    • Cox, J. et al. A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat. Protoc. 4, 698-705 (2009).
    • (2009) Nat. Protoc. , vol.4 , pp. 698-705
    • Cox, J.1
  • 40
    • 67650725988 scopus 로고    scopus 로고
    • Computational principles of determining and improving mass precision and accuracy for proteome measurements in an orbitrap
    • Cox, J. & Mann, M. Computational principles of determining and improving mass precision and accuracy for proteome measurements in an Orbitrap. J. Am. Soc. Mass. Spectrom. 20, 1477-1485 (2009).
    • (2009) J. Am. Soc. Mass. Spectrom. , vol.20 , pp. 1477-1485
    • Cox, J.1    Mann, M.2
  • 41
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski, J.R., Zougman, A., Nagaraj, N. & Mann, M. Universal sample preparation method for proteome analysis. Nat. Methods 6, 359-362 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 42
    • 71549117585 scopus 로고    scopus 로고
    • Combination of fasp and stagetip-based fractionation allows in-depth analysis of the hippocampal membrane proteome
    • Wisniewski, J.R., Zougman, A. & Mann, M. Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome. J. Proteome Res. 8, 5674-5678 (2009).
    • (2009) J. Proteome Res. , vol.8 , pp. 5674-5678
    • Wisniewski, J.R.1    Zougman, A.2    Mann, M.3
  • 43
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification enrichment pre-fractionation and storage of peptides for proteomics using stagetips
    • Rappsilber, J., Mann, M. & Ishihama, Y. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2, 1896-1906 (2007).
    • (2007) Nat. Protoc. , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 44
    • 52649167339 scopus 로고    scopus 로고
    • Prevention of amino acid conversion in silac experiments with embryonic stem cells
    • Bendall, S.C. et al. Prevention of amino acid conversion in SILAC experiments with embryonic stem cells. Mol. Cell. Proteomics 7, 1587-1597 (2008).
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1587-1597
    • Bendall, S.C.1


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