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Volumn 806, Issue , 2014, Pages 93-106

Stable isotope labeling by amino acids in cell culture (SILAC) for quantitative proteomics

Author keywords

[No Author keywords available]

Indexed keywords

ACCURACY; ARTICLE; CELL CULTURE; CELL LABELING; HUMAN; INTERMETHOD COMPARISON; ISOTOPE LABELING; MOLECULAR STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DETERMINATION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN SYNTHESIS; PROTEOMICS; QUANTITATIVE ANALYSIS; SIGNAL TRANSDUCTION; STABLE ISOTOPE LABELING BY AMINO ACID IN CELL CULTURE; CULTURE TECHNIQUE; METABOLISM; METHODOLOGY; REVIEW;

EID: 84907423820     PISSN: 00652598     EISSN: 22148019     Source Type: Book Series    
DOI: 10.1007/978-3-319-06068-2_5     Document Type: Article
Times cited : (30)

References (118)
  • 2
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using aminereactive isobaric tagging reagents
    • Ross PL (2004) Multiplexed protein quantitation in Saccharomyces cerevisiae using aminereactive isobaric tagging reagents. Mol Cell Proteomics 3:1154-1169
    • (2004) Mol Cell Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1
  • 5
    • 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, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M (2002) 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) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 6
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • Ong S, Foster LJ, Mann M (2003) Mass spectrometric-based approaches in quantitative proteomics. Methods 29:124-130
    • (2003) Methods , vol.29 , pp. 124-130
    • Ong, S.1    Foster, L.J.2    Mann, M.3
  • 7
    • 0033535961 scopus 로고    scopus 로고
    • Accurate quantitation of protein expression and site-specific phosphorylation
    • Oda Y, Huang K, Cross FR, Cowburn D, Chait BT (1999) Accurate quantitation of protein expression and site-specific phosphorylation. Proc Natl Acad Sci U S A 96:6591-6596
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6591-6596
    • Oda, Y.1    Huang, K.2    Cross, F.R.3    Cowburn, D.4    Chait, B.T.5
  • 8
    • 79956315121 scopus 로고    scopus 로고
    • Fully automated software solution for protein quantitation by global metabolic labeling with stable isotopes
    • Bindschedler LV, Cramer R (2011) Fully automated software solution for protein quantitation by global metabolic labeling with stable isotopes. Rapid Commun Mass Spectrom 25: 1461-1471
    • (2011) Rapid Commun Mass Spectrom , vol.25 , pp. 1461-1471
    • Bindschedler, L.V.1    Cramer, R.2
  • 10
    • 0242569349 scopus 로고    scopus 로고
    • A proteomic approach for quantitation of phosphorylation using stable isotope labeling in cell culture
    • Ibarrola N, Kalume DE, Gronborg M, Iwahori A, Pandey A (2003) A proteomic approach for quantitation of phosphorylation using stable isotope labeling in cell culture. Anal Chem 75:6043-6049
    • (2003) Anal Chem , vol.75 , pp. 6043-6049
    • Ibarrola, N.1    Kalume, D.E.2    Gronborg, M.3    Iwahori, A.4    Pandey, A.5
  • 11
    • 33748344291 scopus 로고    scopus 로고
    • Quantification of change in phosphorylation of BCR-ABL kinase and its substrates in response to Imatinib treatment in human chronic myelogenous leukemia cells
    • Liang X, Hajivandi M, Veach D, Wisniewski D, Clarkson B, Resh MD, Pope RM (2006) Quantification of change in phosphorylation of BCR-ABL kinase and its substrates in response to Imatinib treatment in human chronic myelogenous leukemia cells. Proteomics 6:4554-4564
    • (2006) Proteomics , vol.6 , pp. 4554-4564
    • Liang, X.1    Hajivandi, M.2    Veach, D.3    Wisniewski, D.4    Clarkson, B.5    Resh, M.D.6    Pope, R.M.7
  • 12
    • 33747592823 scopus 로고    scopus 로고
    • Graded regulation of the Kv2.1 potassium channel by variable phosphorylation
    • Park K, Mohapatra DP, Misonou H, Trimmer JS (2006) Graded regulation of the Kv2.1 potassium channel by variable phosphorylation. Science 313:976-979
    • (2006) Science , vol.313 , pp. 976-979
    • Park, K.1    Mohapatra, D.P.2    Misonou, H.3    Trimmer, J.S.4
  • 13
    • 57349161921 scopus 로고    scopus 로고
    • Constitutive and dynamic phosphorylation and acetylation sites on NUCKS, a hypermodified nuclear protein, studied by quantitative proteomics
    • Wisniewski JR, Zougman A, Krüger S, Ziółkowski P, Pudełko M, Bebenek M, Mann M (2008) Constitutive and dynamic phosphorylation and acetylation sites on NUCKS, a hypermodified nuclear protein, studied by quantitative proteomics. Proteins 73:710-718
    • (2008) Proteins , vol.73 , pp. 710-718
    • Wisniewski, J.R.1    Zougman, A.2    Krüger, S.3    Ziółkowski, P.4    Pudełko, M.5    Bebenek, M.6    Mann, M.7
  • 14
    • 70350770704 scopus 로고    scopus 로고
    • Effect of insulin levels on the phosphorylation of specific amino acid residues in IRS-1: Implications for burn-induced insulin resistance
    • Lu X, Hamrahi VF, Tompkins RG, Fischman AJ (2009) Effect of insulin levels on the phosphorylation of specific amino acid residues in IRS-1: implications for burn-induced insulin resistance. Int J Mol Med 24:531-538
    • (2009) Int J Mol Med , vol.24 , pp. 531-538
    • Lu, X.1    Hamrahi, V.F.2    Tompkins, R.G.3    Fischman, A.J.4
  • 15
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127:635-648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 16
    • 70349329844 scopus 로고    scopus 로고
    • Phosphoproteomics-finally fulfilling the promise?
    • Rogers LD, Foster LJ (2009) Phosphoproteomics-finally fulfilling the promise? Mol Biosyst 5:1122-1129
    • (2009) Mol Biosyst , vol.5 , pp. 1122-1129
    • Rogers, L.D.1    Foster, L.J.2
  • 17
    • 84855932755 scopus 로고    scopus 로고
    • Advances in quantitative phosphoproteomics
    • Nilsson CL (2012) Advances in quantitative phosphoproteomics. Anal Chem 84:735-746
    • (2012) Anal Chem , vol.84 , pp. 735-746
    • Nilsson, C.L.1
  • 18
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible isolation of distinct, overlapping segments of the phosphoproteome
    • Bodenmiller B, Mueller LN, Mueller M, Domon B, Aebersold R (2007) Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nat Methods 4:231-237
    • (2007) Nat Methods , vol.4 , pp. 231-237
    • Bodenmiller, B.1    Mueller, L.N.2    Mueller, M.3    Domon, B.4    Aebersold, R.5
  • 19
    • 0035258256 scopus 로고    scopus 로고
    • Characterization of phosphoproteins from electrophoretic gels by nanoscale Fe(III) affinity chromatography with off-line mass spectrometry analysis
    • Stensballe A, Andersen S, Jensen ON (2001) Characterization of phosphoproteins from electrophoretic gels by nanoscale Fe(III) affinity chromatography with off-line mass spectrometry analysis. Proteomics 1:207-222
    • (2001) Proteomics , vol.1 , pp. 207-222
    • Stensballe, A.1    Andersen, S.2    Jensen, O.N.3
  • 20
    • 0037501375 scopus 로고    scopus 로고
    • Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosincontaining protein/p97 during capacitation
    • Ficarro S, Chertihin O, Westbrook VA, White F, Jayes F, Kalab P, Marto JA, Shabanowitz J, Herr JC, Hunt DF, Visconti PE (2003) Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosincontaining protein/p97 during capacitation. J Biol Chem 278:11579-11589
    • (2003) J Biol Chem , vol.278 , pp. 11579-11589
    • Ficarro, S.1    Chertihin, O.2    Westbrook, V.A.3    White, F.4    Jayes, F.5    Kalab, P.6    Marto, J.A.7    Shabanowitz, J.8    Herr, J.C.9    Hunt, D.F.10    Visconti, P.E.11
  • 21
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen MR, Thingholm TE, Jensen ON, Roepstorff P, Jørgensen TJD (2005) Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol Cell Proteomics 4:873-886
    • (2005) Mol Cell Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jørgensen, T.J.D.5
  • 23
    • 82755163975 scopus 로고    scopus 로고
    • Comparison of three quantitative phosphoproteomic strategies to study receptor tyrosine kinase signaling
    • Zhang G, Neubert TA (2011) Comparison of three quantitative phosphoproteomic strategies to study receptor tyrosine kinase signaling. J Proteome Res 10:5454-5462
    • (2011) J Proteome Res , vol.10 , pp. 5454-5462
    • Zhang, G.1    Neubert, T.A.2
  • 25
    • 65249142741 scopus 로고    scopus 로고
    • Use of differential isotopic labeling and mass spectrometry to analyze capacitation-associated changes in the phosphorylation status of mouse sperm proteins
    • Platt MD, Salicioni AM, Hunt DF, Visconti PE (2009) Use of differential isotopic labeling and mass spectrometry to analyze capacitation-associated changes in the phosphorylation status of mouse sperm proteins. J Proteome Res 8:1431-1440
    • (2009) J Proteome Res , vol.8 , pp. 1431-1440
    • Platt, M.D.1    Salicioni, A.M.2    Hunt, D.F.3    Visconti, P.E.4
  • 26
    • 84859562238 scopus 로고    scopus 로고
    • Global analysis of phosphoproteome regulation by the Ser/Thr phosphatase Ppt1 in Saccharomyces cerevisiae
    • Schreiber TB, Mäusbacher N, Soroka J, Wandinger SK, Buchner J, Daub H (2012) Global analysis of phosphoproteome regulation by the Ser/Thr phosphatase Ppt1 in Saccharomyces cerevisiae. J Proteome Res 11:2397-2408
    • (2012) J Proteome Res , vol.11 , pp. 2397-2408
    • Schreiber, T.B.1    Mäusbacher, N.2    Soroka, J.3    Wandinger, S.K.4    Buchner, J.5    Daub, H.6
  • 27
    • 84870391451 scopus 로고    scopus 로고
    • Comparative phosphoproteomics studies of macrophage response to bacterial virulence effectors
    • Chen C, Wu D, Zhang L, Zhao Y, Guo L (2012) Comparative phosphoproteomics studies of macrophage response to bacterial virulence effectors. J Proteomics 77:251-261
    • (2012) J Proteomics , vol.77 , pp. 251-261
    • Chen, C.1    Wu, D.2    Zhang, L.3    Zhao, Y.4    Guo, L.5
  • 29
    • 70349621112 scopus 로고    scopus 로고
    • Systems-wide analysis of a phosphatase knockdown by quantitative proteomics and phosphoproteomics
    • Hilger M, Bonaldi T, Gnad F, Mann M (2009) Systems-wide analysis of a phosphatase knockdown by quantitative proteomics and phosphoproteomics. Mol Cell Proteomics 8:1908-1920
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1908-1920
    • Hilger, M.1    Bonaldi, T.2    Gnad, F.3    Mann, M.4
  • 30
    • 84877131327 scopus 로고    scopus 로고
    • Global quantitative SILAC phosphoproteomics reveals differential phosphorylation is widespread between the procyclic and bloodstream form lifecycle stages of Trypanosoma brucei
    • Urbaniak MD, Martin DMA, Ferguson MAJ (2013) Global quantitative SILAC phosphoproteomics reveals differential phosphorylation is widespread between the procyclic and bloodstream form lifecycle stages of Trypanosoma brucei. J Proteome Res 12:2233-2244
    • (2013) J Proteome Res , vol.12 , pp. 2233-2244
    • Urbaniak, M.D.1    Martin, D.M.A.2    Ferguson, M.A.J.3
  • 31
    • 72449196261 scopus 로고    scopus 로고
    • Global effects of kinase inhibitors on signaling networks revealed by quantitative phosphoproteomics
    • Pan C, Olsen JV, Daub H, Mann M (2009) Global effects of kinase inhibitors on signaling networks revealed by quantitative phosphoproteomics. Mol Cell Proteomics 8:2796-2808
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2796-2808
    • Pan, C.1    Olsen, J.V.2    Daub, H.3    Mann, M.4
  • 33
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyrosinedependent signaling networks by quantitative proteomics
    • Blagoev B, Ong S, Kratchmarova I, Mann M (2004) Temporal analysis of phosphotyrosinedependent signaling networks by quantitative proteomics. Nat Biotechnol 22:1139-1145
    • (2004) Nat Biotechnol , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.2    Kratchmarova, I.3    Mann, M.4
  • 35
    • 8744253743 scopus 로고    scopus 로고
    • Tyrosine phosphoproteomics of fibroblast growth factor signaling: A role for insulin receptor substrate-4
    • Hinsby AM, Olsen JV, Mann M (2004) Tyrosine phosphoproteomics of fibroblast growth factor signaling: a role for insulin receptor substrate-4. J Biol Chem 279:46438-46447
    • (2004) J Biol Chem , vol.279 , pp. 46438-46447
    • Hinsby, A.M.1    Olsen, J.V.2    Mann, M.3
  • 36
    • 77952037166 scopus 로고    scopus 로고
    • Differential phosphoproteomics of fibroblast growth factor signaling: Identification of Src family kinase-mediated phosphorylation events
    • Cunningham DL, Sweet SMM, Cooper HJ, Heath JK (2010) Differential phosphoproteomics of fibroblast growth factor signaling: identification of Src family kinase-mediated phosphorylation events. J Proteome Res 9:2317-2328
    • (2010) J Proteome Res , vol.9 , pp. 2317-2328
    • Cunningham, D.L.1    Sweet, S.M.M.2    Cooper, H.J.3    Heath, J.K.4
  • 37
    • 20344363684 scopus 로고    scopus 로고
    • Mechanism of divergent growth factor effects in mesenchymal stem cell differentiation
    • Kratchmarova I, Blagoev B, Haack-Sorensen M, Kassem M, Mann M (2005) Mechanism of divergent growth factor effects in mesenchymal stem cell differentiation. Science 308: 1472-1477
    • (2005) Science , vol.308 , pp. 1472-1477
    • Kratchmarova, I.1    Blagoev, B.2    Haack-Sorensen, M.3    Kassem, M.4    Mann, M.5
  • 38
    • 33644836196 scopus 로고    scopus 로고
    • Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC)
    • Zhang G, Spellman DS, Skolnik EY, Neubert TA (2006) Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC). J Proteome Res 5:581-588
    • (2006) J Proteome Res , vol.5 , pp. 581-588
    • Zhang, G.1    Spellman, D.S.2    Skolnik, E.Y.3    Neubert, T.A.4
  • 40
    • 45749144385 scopus 로고    scopus 로고
    • Stable isotopic labeling by amino acids in cultured primary neurons: Application to brain-derived neurotrophic factordependent phosphotyrosine-associated signaling
    • Spellman DS, Deinhardt K, Darie CC, Chao MV, Neubert TA (2008) Stable isotopic labeling by amino acids in cultured primary neurons: application to brain-derived neurotrophic factordependent phosphotyrosine-associated signaling. Mol Cell Proteomics 7:1067-1076
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1067-1076
    • Spellman, D.S.1    Deinhardt, K.2    Darie, C.C.3    Chao, M.V.4    Neubert, T.A.5
  • 43
    • 84883197055 scopus 로고    scopus 로고
    • Quantitative profiling of tyrosine phosphorylation revealed changes in the activity of the T cell receptor signaling pathway upon cisplatin-induced apoptosis
    • Størvold GL, Landskron J, Strozynski M, Arntzen MØ, Koehler CJ, Kalland ME, Taskén K, Thiede B (2013) Quantitative profiling of tyrosine phosphorylation revealed changes in the activity of the T cell receptor signaling pathway upon cisplatin-induced apoptosis. J Proteomics 91:344-357
    • (2013) J Proteomics , vol.91 , pp. 344-357
    • Størvold, G.L.1    Landskron, J.2    Strozynski, M.3    Arntzen, M.Ø.4    Koehler, C.J.5    Kalland, M.E.6    Taskén, K.7    Thiede, B.8
  • 44
    • 26844576371 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules
    • Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM (2005) Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics 4:1240-1250
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1240-1250
    • Zhang, Y.1    Wolf-Yadlin, A.2    Ross, P.L.3    Pappin, D.J.4    Rush, J.5    Lauffenburger, D.A.6    White, F.M.7
  • 45
    • 73649134351 scopus 로고    scopus 로고
    • Hyperglycemia alters the schwann cell mitochondrial proteome and decreases coupled respiration in the absence of superoxide production
    • Zhang L, Yu C, Vasquez FE, Galeva N, Onyango I, Swerdlow RH, Dobrowsky RT (2010) Hyperglycemia alters the schwann cell mitochondrial proteome and decreases coupled respiration in the absence of superoxide production. J Proteome Res 9:458-471
    • (2010) J Proteome Res , vol.9 , pp. 458-471
    • Zhang, L.1    Yu, C.2    Vasquez, F.E.3    Galeva, N.4    Onyango, I.5    Swerdlow, R.H.6    Dobrowsky, R.T.7
  • 46
    • 77956742502 scopus 로고    scopus 로고
    • Identification of BCAP-(L) as a negative regulator of the TLR signaling-induced production of IL-6 and IL-10 in macrophages by tyrosine phosphoproteomics
    • Matsumura T, Oyama M, Kozuka-Hata H, Ishikawa K, Inoue T, Muta T, Semba K, Inoue J (2010) Identification of BCAP-(L) as a negative regulator of the TLR signaling-induced production of IL-6 and IL-10 in macrophages by tyrosine phosphoproteomics. Biochem Biophys Res Commun 400:265-270
    • (2010) Biochem Biophys Res Commun , vol.400 , pp. 265-270
    • Matsumura, T.1    Oyama, M.2    Kozuka-Hata, H.3    Ishikawa, K.4    Inoue, T.5    Muta, T.6    Semba, K.7    Inoue, J.8
  • 49
    • 84871259137 scopus 로고    scopus 로고
    • Proteome-wide analysis of temporal phosphorylation dynamics in lysophosphatidic acid-induced signaling
    • Mäusbacher N, Schreiber TB, Machatti M, Schaab C, Daub H (2012) Proteome-wide analysis of temporal phosphorylation dynamics in lysophosphatidic acid-induced signaling. Proteomics 12:3485-3498
    • (2012) Proteomics , vol.12 , pp. 3485-3498
    • Mäusbacher, N.1    Schreiber, T.B.2    Machatti, M.3    Schaab, C.4    Daub, H.5
  • 50
    • 84875022084 scopus 로고    scopus 로고
    • Global protein phosphorylation dynamics during deoxynivalenol-induced ribotoxic stress response in the macrophage
    • Pan X, Whitten DA, Wu M, Chan C, Wilkerson CG, Pestka JJ (2013) Global protein phosphorylation dynamics during deoxynivalenol-induced ribotoxic stress response in the macrophage. Toxicol Appl Pharmacol 268:201-211
    • (2013) Toxicol Appl Pharmacol , vol.268 , pp. 201-211
    • Pan, X.1    Whitten, D.A.2    Wu, M.3    Chan, C.4    Wilkerson, C.G.5    Pestka, J.J.6
  • 51
    • 77649138161 scopus 로고    scopus 로고
    • Screening for therapeutic targets of vorinostat by SILAC-based proteomic analysis in human breast cancer cells
    • Zhou Q, Chaerkady R, Shaw PG, Kensler TW, Pandey A, Davidson NE (2010) Screening for therapeutic targets of vorinostat by SILAC-based proteomic analysis in human breast cancer cells. Proteomics 10:1029-1039
    • (2010) Proteomics , vol.10 , pp. 1029-1039
    • Zhou, Q.1    Chaerkady, R.2    Shaw, P.G.3    Kensler, T.W.4    Pandey, A.5    Davidson, N.E.6
  • 52
    • 84878524313 scopus 로고    scopus 로고
    • Acetylation dynamics of human nuclear proteins during the ionizing radiation-induced DNA damage response
    • Bennetzen MV, Larsen DH, Dinant C, Watanabe S, Bartek J, Lukas J, Andersen JS (2013) Acetylation dynamics of human nuclear proteins during the ionizing radiation-induced DNA damage response. Cell Cycle 12:1688-1695
    • (2013) Cell Cycle , vol.12 , pp. 1688-1695
    • Bennetzen, M.V.1    Larsen, D.H.2    Dinant, C.3    Watanabe, S.4    Bartek, J.5    Lukas, J.6    Andersen, J.S.7
  • 53
    • 84883750603 scopus 로고    scopus 로고
    • SAHA treatment reveals the link between histone lysine acetylation and proteome in nonsmall cell lung cancer A549 Cells
    • Wu Q, Xu W, Cao L, Li X, He T, Wu Z, Li W (2013) SAHA treatment reveals the link between histone lysine acetylation and proteome in nonsmall cell lung cancer A549 Cells. J Proteome Res 12:4064-4073
    • (2013) J Proteome Res , vol.12 , pp. 4064-4073
    • Wu, Q.1    Xu, W.2    Cao, L.3    Li, X.4    He, T.5    Wu, Z.6    Li, W.7
  • 54
    • 55949136614 scopus 로고    scopus 로고
    • Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry
    • Meierhofer D, Wang X, Huang L, Kaiser P (2008) Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res 7:4566-4576
    • (2008) J Proteome Res , vol.7 , pp. 4566-4576
    • Meierhofer, D.1    Wang, X.2    Huang, L.3    Kaiser, P.4
  • 55
    • 80755175389 scopus 로고    scopus 로고
    • Characterization of ubiquitination dependent dynamics in growth factor receptor signaling by quantitative proteomics
    • Akimov V, Rigbolt KTG, Nielsen MM, Blagoev B (2011) Characterization of ubiquitination dependent dynamics in growth factor receptor signaling by quantitative proteomics. Mol Biosyst 7:3223-3233
    • (2011) Mol Biosyst , vol.7 , pp. 3223-3233
    • Akimov, V.1    Rigbolt, K.T.G.2    Nielsen, M.M.3    Blagoev, B.4
  • 56
    • 84864131300 scopus 로고    scopus 로고
    • Analysis of ubiquitinated proteome by quantitative mass spectrometry
    • Na CH, Peng J (2012) Analysis of ubiquitinated proteome by quantitative mass spectrometry. Methods Mol Biol 893:417-429
    • (2012) Methods Mol Biol , vol.893 , pp. 417-429
    • Na, C.H.1    Peng, J.2
  • 57
    • 84885012783 scopus 로고    scopus 로고
    • Large-scale identification of ubiquitination sites by mass spectrometry
    • Udeshi ND, Mertins P, Svinkina T, Carr SA (2013) Large-scale identification of ubiquitination sites by mass spectrometry. Nat Protoc 8:1950-1960
    • (2013) Nat Protoc , vol.8 , pp. 1950-1960
    • Udeshi, N.D.1    Mertins, P.2    Svinkina, T.3    Carr, S.A.4
  • 58
    • 84891801891 scopus 로고    scopus 로고
    • Peptide level immunoaffinity enrichment enhances ubiquitination site identification on individual proteins
    • Anania VG, Pham VC, Huang X, Masselot A, Lill JR, Kirkpatrick DS (2014) Peptide level immunoaffinity enrichment enhances ubiquitination site identification on individual proteins. Mol Cell Proteomics 13(1):145-156
    • (2014) Mol Cell Proteomics , vol.13 , Issue.1 , pp. 145-156
    • Anania, V.G.1    Pham, V.C.2    Huang, X.3    Masselot, A.4    Lill, J.R.5    Kirkpatrick, D.S.6
  • 60
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong S, Mittler G, Mann M (2004) Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nat Methods 1:119-126
    • (2004) Nat Methods , vol.1 , pp. 119-126
    • Ong, S.1    Mittler, G.2    Mann, M.3
  • 61
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong S, Mann M (2006) A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat Protoc 1:2650-2660
    • (2006) Nat Protoc , vol.1 , pp. 2650-2660
    • Ong, S.1    Mann, M.2
  • 64
    • 84881010295 scopus 로고    scopus 로고
    • Heavy methyl-SILAC labeling coupled with liquid chromatography and high-resolution mass spectrometry to study the dynamics of site-specific histone methylation
    • Cao X, Zee BM, Garcia BA (2013) Heavy methyl-SILAC labeling coupled with liquid chromatography and high-resolution mass spectrometry to study the dynamics of site-specific histone methylation. Methods Mol Biol 977:299-313
    • (2013) Methods Mol Biol , vol.977 , pp. 299-313
    • Cao, X.1    Zee, B.M.2    Garcia, B.A.3
  • 65
    • 34548438595 scopus 로고    scopus 로고
    • Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation
    • Wang Z, Pandey A, Hart GW (2007) Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation. Mol Cell Proteomics 6:1365-1379
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1365-1379
    • Wang, Z.1    Pandey, A.2    Hart, G.W.3
  • 66
    • 77954378942 scopus 로고    scopus 로고
    • Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry
    • Ostasiewicz P, Zielinska DF, Mann M, Wisniewski JR (2010) Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry. J Proteome Res 9:3688-3700
    • (2010) J Proteome Res , vol.9 , pp. 3688-3700
    • Ostasiewicz, P.1    Zielinska, D.F.2    Mann, M.3    Wisniewski, J.R.4
  • 67
    • 80052378239 scopus 로고    scopus 로고
    • Titanium dioxide enrichment of sialic acidcontaining glycopeptides
    • Palmisano G, Lendal SE, Larsen MR (2011) Titanium dioxide enrichment of sialic acidcontaining glycopeptides. Methods Mol Biol 753:309-322
    • (2011) Methods Mol Biol , vol.753 , pp. 309-322
    • Palmisano, G.1    Lendal, S.E.2    Larsen, M.R.3
  • 68
    • 84871860708 scopus 로고    scopus 로고
    • Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples
    • Boersema PJ, Geiger T, Wisniewski JR, Mann M (2013) Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples. Mol Cell Proteomics 12:158-171
    • (2013) Mol Cell Proteomics , vol.12 , pp. 158-171
    • Boersema, P.J.1    Geiger, T.2    Wisniewski, J.R.3    Mann, M.4
  • 69
    • 84877108318 scopus 로고    scopus 로고
    • Site-specific quantitative analysis of overglycosylation of collagen in osteogenesis imperfecta using hydrazide chemistry and SILAC
    • Taga Y, Kusubata M, Ogawa-Goto K, Hattori S (2013) Site-specific quantitative analysis of overglycosylation of collagen in osteogenesis imperfecta using hydrazide chemistry and SILAC. J Proteome Res 12:2225-2232
    • (2013) J Proteome Res , vol.12 , pp. 2225-2232
    • Taga, Y.1    Kusubata, M.2    Ogawa-Goto, K.3    Hattori, S.4
  • 70
    • 36749030517 scopus 로고    scopus 로고
    • Analysis of dynamic changes in post-translational modifications of human histones during cell cycle by mass spectrometry
    • Bonenfant D, Towbin H, Coulot M, Schindler P, Mueller DR, van Oostrum J (2007) Analysis of dynamic changes in post-translational modifications of human histones during cell cycle by mass spectrometry. Mol Cell Proteomics 6:1917-1932
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1917-1932
    • Bonenfant, D.1    Towbin, H.2    Coulot, M.3    Schindler, P.4    Mueller, D.R.5    van Oostrum, J.6
  • 71
    • 79960281535 scopus 로고    scopus 로고
    • SILAC-based proteomic analysis to dissect the "histone modification signature" of human breast cancer cells
    • Cuomo A, Moretti S, Minucci S, Bonaldi T (2011) SILAC-based proteomic analysis to dissect the "histone modification signature" of human breast cancer cells. Amino Acids 41:387-399
    • (2011) Amino Acids , vol.41 , pp. 387-399
    • Cuomo, A.1    Moretti, S.2    Minucci, S.3    Bonaldi, T.4
  • 72
    • 84881114088 scopus 로고    scopus 로고
    • Discovery of histone modification crosstalk networks by stable isotope labeling of amino acids in cell culture mass spectrometry (SILAC MS)
    • Guan X, Rastogi N, Parthun MR, Freitas MA (2013) Discovery of histone modification crosstalk networks by stable isotope labeling of amino acids in cell culture mass spectrometry (SILAC MS). Mol Cell Proteomics 12:2048-2059
    • (2013) Mol Cell Proteomics , vol.12 , pp. 2048-2059
    • Guan, X.1    Rastogi, N.2    Parthun, M.R.3    Freitas, M.A.4
  • 74
    • 78651487556 scopus 로고    scopus 로고
    • The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC
    • Zhong J, Chaerkady R, Kandasamy K, Gucek M, Cole RN, Pandey A (2011) The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC. J Proteomics 74: 294-303
    • (2011) J Proteomics , vol.74 , pp. 294-303
    • Zhong, J.1    Chaerkady, R.2    Kandasamy, K.3    Gucek, M.4    Cole, R.N.5    Pandey, A.6
  • 75
    • 30744464873 scopus 로고    scopus 로고
    • Insulin-dependent interactions of proteins with GLUT4 revealed through stable isotope labeling by amino acids in cell culture (SILAC)
    • Foster LJ, Rudich A, Talior I, Patel N, Huang X, Furtado LM, Bilan PJ, Mann M, Klip A (2006) Insulin-dependent interactions of proteins with GLUT4 revealed through stable isotope labeling by amino acids in cell culture (SILAC). J Proteome Res 5:64-75
    • (2006) J Proteome Res , vol.5 , pp. 64-75
    • Foster, L.J.1    Rudich, A.2    Talior, I.3    Patel, N.4    Huang, X.5    Furtado, L.M.6    Bilan, P.J.7    Mann, M.8    Klip, A.9
  • 76
    • 63049091804 scopus 로고    scopus 로고
    • The phosphotyrosine interactome of the insulin receptor family and its substrates IRS-1 and IRS-2
    • Hanke S, Mann M (2009) The phosphotyrosine interactome of the insulin receptor family and its substrates IRS-1 and IRS-2. Mol Cell Proteomics 8:519-534
    • (2009) Mol Cell Proteomics , vol.8 , pp. 519-534
    • Hanke, S.1    Mann, M.2
  • 77
    • 40849108777 scopus 로고    scopus 로고
    • Mapping the integrin-linked kinase interactome using SILAC
    • Dobreva I, Fielding A, Foster LJ, Dedhar S (2008) Mapping the integrin-linked kinase interactome using SILAC. J Proteome Res 7:1740-1749
    • (2008) J Proteome Res , vol.7 , pp. 1740-1749
    • Dobreva, I.1    Fielding, A.2    Foster, L.J.3    Dedhar, S.4
  • 78
    • 77952023070 scopus 로고    scopus 로고
    • Quantitative analysis of kinase-proximal signaling in lipopolysaccharide-induced innate immune response
    • Sharma K, Kumar C, Kéri G, Breitkopf SB, Oppermann FS, Daub H (2010) Quantitative analysis of kinase-proximal signaling in lipopolysaccharide-induced innate immune response. J Proteome Res 9:2539-2549
    • (2010) J Proteome Res , vol.9 , pp. 2539-2549
    • Sharma, K.1    Kumar, C.2    Kéri, G.3    Breitkopf, S.B.4    Oppermann, F.S.5    Daub, H.6
  • 80
    • 48249094218 scopus 로고    scopus 로고
    • Discrimination between stable and dynamic components of protein complexes by means of quantitative proteomics
    • Kito K, Kawaguchi N, Okada S, Ito T (2008) Discrimination between stable and dynamic components of protein complexes by means of quantitative proteomics. Proteomics 8: 2366-2370
    • (2008) Proteomics , vol.8 , pp. 2366-2370
    • Kito, K.1    Kawaguchi, N.2    Okada, S.3    Ito, T.4
  • 81
    • 58149344947 scopus 로고    scopus 로고
    • Comparative multiplexed mass spectrometric analyses of endogenously expressed yeast nuclear and cytoplasmic exosomes
    • Synowsky SA, van Wijk M, Raijmakers R, Heck AJR (2009) Comparative multiplexed mass spectrometric analyses of endogenously expressed yeast nuclear and cytoplasmic exosomes. J Mol Biol 385:1300-1313
    • (2009) J Mol Biol , vol.385 , pp. 1300-1313
    • Synowsky, S.A.1    van Wijk, M.2    Raijmakers, R.3    Heck, A.J.R.4
  • 82
    • 80355130499 scopus 로고    scopus 로고
    • Identification of protein complexes with quantitative proteomics in S. cerevisiae
    • pii: 1225
    • Chao JT, Foster LJ, Loewen CJR (2009) Identification of protein complexes with quantitative proteomics in S. cerevisiae. J Vis Exp (25). pii: 1225
    • (2009) J Vis Exp , vol.25
    • Chao, J.T.1    Foster, L.J.2    Loewen, C.J.R.3
  • 84
    • 33751230224 scopus 로고    scopus 로고
    • Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK)
    • Selbach M, Mann M (2006) Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK). Nat Methods 3:981-983
    • (2006) Nat Methods , vol.3 , pp. 981-983
    • Selbach, M.1    Mann, M.2
  • 85
    • 78149396586 scopus 로고    scopus 로고
    • Identification of novel 14-3-3ζ interacting proteins by quantitative immunoprecipitation combined with knockdown (QUICK)
    • Ge F, Li W, Bi L, Tao S, Zhang Z, Zhang X (2010) Identification of novel 14-3-3ζ interacting proteins by quantitative immunoprecipitation combined with knockdown (QUICK). J Proteome Res 9:5848-5858
    • (2010) J Proteome Res , vol.9 , pp. 5848-5858
    • Ge, F.1    Li, W.2    Bi, L.3    Tao, S.4    Zhang, Z.5    Zhang, X.6
  • 87
    • 77953140591 scopus 로고    scopus 로고
    • A role for BAF57 in cell cycle-dependent transcriptional regulation by the SWI/SNF chromatin remodeling complex
    • Hah N, Kolkman A, Ruhl DD, Pijnappel WWMP, Heck AJR, Timmers HTM, Kraus WL (2010) A role for BAF57 in cell cycle-dependent transcriptional regulation by the SWI/SNF chromatin remodeling complex. Cancer Res 70:4402-4411
    • (2010) Cancer Res , vol.70 , pp. 4402-4411
    • Hah, N.1    Kolkman, A.2    Ruhl, D.D.3    Pijnappel, W.W.M.P.4    Heck, A.J.R.5    Timmers, H.T.M.6    Kraus, W.L.7
  • 88
    • 84355166425 scopus 로고    scopus 로고
    • QUICK identification and SPR validation of signal transducers and activators of transcription 3 (Stat3) interacting proteins
    • Zheng P, Zhong Q, Xiong Q, Yang M, Zhang J, Li C, Bi L, Ge F (2012) QUICK identification and SPR validation of signal transducers and activators of transcription 3 (Stat3) interacting proteins. J Proteomics 75:1055-1066
    • (2012) J Proteomics , vol.75 , pp. 1055-1066
    • Zheng, P.1    Zhong, Q.2    Xiong, Q.3    Yang, M.4    Zhang, J.5    Li, C.6    Bi, L.7    Ge, F.8
  • 89
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev B, Kratchmarova I, Ong S, Nielsen M, Foster LJ, Mann M (2003) A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat Biotechnol 21:315-318
    • (2003) Nat Biotechnol , vol.21 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 91
    • 13844317869 scopus 로고    scopus 로고
    • Proteome dynamics in complex organisms: Using stable isotopes to monitor individual protein turnover rates
    • Doherty MK, Whitehead C, McCormack H, Gaskell SJ, Beynon RJ (2005) Proteome dynamics in complex organisms: using stable isotopes to monitor individual protein turnover rates. Proteomics 5:522-533
    • (2005) Proteomics , vol.5 , pp. 522-533
    • Doherty, M.K.1    Whitehead, C.2    McCormack, H.3    Gaskell, S.J.4    Beynon, R.J.5
  • 92
    • 60849097304 scopus 로고    scopus 로고
    • Turnover of the human proteome: Determination of protein intracellular stability by dynamic SILAC
    • Doherty MK, Hammond DE, Clague MJ, Gaskell SJ, Beynon RJ (2009) Turnover of the human proteome: determination of protein intracellular stability by dynamic SILAC. J Proteome Res 8:104-112
    • (2009) J Proteome Res , vol.8 , pp. 104-112
    • Doherty, M.K.1    Hammond, D.E.2    Clague, M.J.3    Gaskell, S.J.4    Beynon, R.J.5
  • 93
    • 33644701579 scopus 로고    scopus 로고
    • The turnover kinetics of major histocompatibility complex peptides of human cancer cells
    • Milner E, Barnea E, Beer I, Admon A (2006) The turnover kinetics of major histocompatibility complex peptides of human cancer cells. Mol Cell Proteomics 5:357-365
    • (2006) Mol Cell Proteomics , vol.5 , pp. 357-365
    • Milner, E.1    Barnea, E.2    Beer, I.3    Admon, A.4
  • 96
    • 0347361590 scopus 로고    scopus 로고
    • Synthesis/degradation ratio mass spectrometry for measuring relative dynamic protein turnover
    • Cargile BJ, Bundy JL, Grunden AM, Stephenson JL (2004) Synthesis/degradation ratio mass spectrometry for measuring relative dynamic protein turnover. Anal Chem 76:86-97
    • (2004) Anal Chem , vol.76 , pp. 86-97
    • Cargile, B.J.1    Bundy, J.L.2    Grunden, A.M.3    Stephenson, J.L.4
  • 98
    • 82755184981 scopus 로고    scopus 로고
    • Systems-wide proteomic analysis in mammalian cells reveals conserved, functional protein turnover
    • Cambridge SB, Gnad F, Nguyen C, Bermejo JL, Krüger M, Mann M (2011) Systems-wide proteomic analysis in mammalian cells reveals conserved, functional protein turnover. J Proteome Res 10:5275-5284
    • (2011) J Proteome Res , vol.10 , pp. 5275-5284
    • Cambridge, S.B.1    Gnad, F.2    Nguyen, C.3    Bermejo, J.L.4    Krüger, M.5    Mann, M.6
  • 101
    • 84867161245 scopus 로고    scopus 로고
    • Temporal profiling and pulsed SILAC labeling identify novel secreted proteins during ex vivo osteoblast differentiation of human stromal stem cells
    • Kristensen LP, Chen L, Nielsen MO, Qanie DW, Kratchmarova I, Kassem M, Andersen JS (2012) Temporal profiling and pulsed SILAC labeling identify novel secreted proteins during ex vivo osteoblast differentiation of human stromal stem cells. Mol Cell Proteomics 11: 989-1007
    • (2012) Mol Cell Proteomics , vol.11 , pp. 989-1007
    • Kristensen, L.P.1    Chen, L.2    Nielsen, M.O.3    Qanie, D.W.4    Kratchmarova, I.5    Kassem, M.6    Andersen, J.S.7
  • 103
    • 59449085150 scopus 로고    scopus 로고
    • Global analysis of cellular protein translation by pulsed SILAC
    • Schwanhäusser B, Gossen M, Dittmar G, Selbach M (2009) Global analysis of cellular protein translation by pulsed SILAC. Proteomics 9:205-209
    • (2009) Proteomics , vol.9 , pp. 205-209
    • Schwanhäusser, B.1    Gossen, M.2    Dittmar, G.3    Selbach, M.4
  • 105
    • 79955791663 scopus 로고    scopus 로고
    • Study of neurotrophin-3 signaling in primary cultured neurons using multiplex stable isotope labeling with amino acids in cell culture
    • Zhang G, Deinhardt K, Chao MV, Neubert TA (2011) Study of neurotrophin-3 signaling in primary cultured neurons using multiplex stable isotope labeling with amino acids in cell culture. J Proteome Res 10:2546-2554
    • (2011) J Proteome Res , vol.10 , pp. 2546-2554
    • Zhang, G.1    Deinhardt, K.2    Chao, M.V.3    Neubert, T.A.4
  • 108
    • 77958018495 scopus 로고    scopus 로고
    • The SILAC fly allows for accurate protein quantification in vivo
    • Sury MD, Chen J, Selbach M (2010) The SILAC fly allows for accurate protein quantification in vivo. Mol Cell Proteomics 9:2173-2183
    • (2010) Mol Cell Proteomics , vol.9 , pp. 2173-2183
    • Sury, M.D.1    Chen, J.2    Selbach, M.3
  • 109
    • 84866066300 scopus 로고    scopus 로고
    • Stable isotope labeling with amino acids in Drosophila for quantifying proteins and modifications
    • Xu P, Tan H, Duong DM, Yang Y, Kupsco J, Moberg KH, Li H, Jin P, Peng J (2012) Stable isotope labeling with amino acids in Drosophila for quantifying proteins and modifications. J Proteome Res 11:4403-4412
    • (2012) J Proteome Res , vol.11 , pp. 4403-4412
    • Xu, P.1    Tan, H.2    Duong, D.M.3    Yang, Y.4    Kupsco, J.5    Moberg, K.H.6    Li, H.7    Jin, P.8    Peng, J.9
  • 111
    • 4444346217 scopus 로고    scopus 로고
    • Metabolic labeling of mammalian organisms with stable isotopes for quantitative proteomic analysis
    • Wu CC, MacCoss MJ, Howell KE, Matthews DE, Yates JR (2004) Metabolic labeling of mammalian organisms with stable isotopes for quantitative proteomic analysis. Anal Chem 76:4951-4959
    • (2004) Anal Chem , vol.76 , pp. 4951-4959
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Matthews, D.E.4    Yates, J.R.5
  • 113
    • 22844436250 scopus 로고    scopus 로고
    • Quantitative mouse brain proteomics using culture-derived isotope tags as internal standards
    • Ishihama Y, Sato T, Tabata T, Miyamoto N, Sagane K, Nagasu T, Oda Y (2005) Quantitative mouse brain proteomics using culture-derived isotope tags as internal standards. Nat Biotechnol 23:617-621
    • (2005) Nat Biotechnol , vol.23 , pp. 617-621
    • Ishihama, Y.1    Sato, T.2    Tabata, T.3    Miyamoto, N.4    Sagane, K.5    Nagasu, T.6    Oda, Y.7
  • 115
    • 84861157792 scopus 로고    scopus 로고
    • Super-SILAC allows classification of diffuse large B-cell lymphoma subtypes by their protein expression profiles
    • Deeb SJ, D'Souza RCJ, Cox J, Schmidt-Supprian M, Mann M (2012) Super-SILAC allows classification of diffuse large B-cell lymphoma subtypes by their protein expression profiles. Mol Cell Proteomics 11:77-89
    • (2012) Mol Cell Proteomics , vol.11 , pp. 77-89
    • Deeb, S.J.1    D'Souza, R.C.J.2    Cox, J.3    Schmidt-Supprian, M.4    Mann, M.5
  • 116
    • 79961014854 scopus 로고    scopus 로고
    • Large-scale phosphosite quantification in tissues by a spike-in SILAC method
    • Monetti M, Nagaraj N, Sharma K, Mann M (2011) Large-scale phosphosite quantification in tissues by a spike-in SILAC method. Nat Methods 8:655-658
    • (2011) Nat Methods , vol.8 , pp. 655-658
    • Monetti, M.1    Nagaraj, N.2    Sharma, K.3    Mann, M.4


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