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Volumn 893, Issue , 2012, Pages 201-221

SILAC for the study of mammalian cell lines and yeast protein complexes

Author keywords

Affinity purification; Mass spectrometry; Protein complex; Protein protein interactions; Quantitative proteomics; Relative protein quantification; Stable isotope labeling; Stable isotope labeling by amino acids in cell culture

Indexed keywords

AMINO ACID; CELL EXTRACT; MULTIPROTEIN COMPLEX; PROTEOME; SACCHAROMYCES CEREVISIAE PROTEIN; TRYPSIN;

EID: 84864139924     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-885-6_14     Document Type: Article
Times cited : (12)

References (41)
  • 1
    • 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 SE, Blagoev B, Kratchmarova I et al (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.E.1    Blagoev, B.2    Kratchmarova, I.3
  • 2
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev B, Kratchmarova I, Ong SE et al (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.E.3
  • 3
    • 67349225422 scopus 로고    scopus 로고
    • New dimensions in the study of protein complexes using quantitative mass spectrometry
    • Oeljeklaus S, Meyer HE, Warscheid B (2009) New dimensions in the study of protein complexes using quantitative mass spectrometry. FEBS Lett 583:1674-1683
    • (2009) FEBS Lett. , vol.583 , pp. 1674-1683
    • Oeljeklaus, S.1    Meyer, H.E.2    Warscheid, B.3
  • 4
    • 39049117451 scopus 로고    scopus 로고
    • Identifying dynamic interactors of protein complexes by quantitative mass spectrometry
    • Wang X, Huang L (2008) Identifying dynamic interactors of protein complexes by quantitative mass spectrometry. Mol Cell Proteomics 7:46-57
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 46-57
    • Wang, X.1    Huang, L.2
  • 5
    • 43849110454 scopus 로고    scopus 로고
    • Quantitative proteomics reveals regulation of dynamic components within TATA-binding protein TBP transcription complexes
    • Mousson F, Kolkman A, Pijnappel WW et al (2008) Quantitative proteomics reveals regulation of dynamic components within TATA-binding protein (TBP) transcription complexes. Mol Cell Proteomics 7:845-852
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 845-852
    • Mousson, F.1    Kolkman, A.2    Pijnappel, W.W.3
  • 6
    • 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 et al (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
  • 7
    • 15944377809 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway
    • Gruhler A, Olsen JV, Mohammed S et al (2005) Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway. Mol Cell Proteomics 4:310-327
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 310-327
    • Gruhler, A.1    Olsen, J.V.2    Mohammed, S.3
  • 8
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong SE, 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.E.1    Mittler, G.2    Mann, M.3
  • 9
    • 57349161921 scopus 로고    scopus 로고
    • Constitutive and dynamic phosphorylation and acetylation sites on NUCKS, a hypermodified nuclear protein, studied by quantitative proteomics
    • Wiśniewski JR, Zougman A, Krüger S et al (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
    • Wiśniewski, J.R.1    Zougman, A.2    Krüger, S.3
  • 10
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C, Kumar C, Gnad F et al (2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325:834-840
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3
  • 11
    • 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
  • 12
    • 70549086229 scopus 로고    scopus 로고
    • Large-scale proteomics analysis of the human kinome
    • Oppermann FS, Gnad F, Olsen JV et al (2009) Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics 8:1751-1764
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1751-1764
    • Oppermann, F.S.1    Gnad, F.2    Olsen, J.V.3
  • 13
    • 77951644400 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis
    • Olsen JV, Vermeulen M, Santamaria A et al (2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal 3(104):ra3
    • (2010) Sci. Signal , vol.3 , Issue.104
    • Olsen, J.V.1    Vermeulen, M.2    Santamaria, A.3
  • 14
    • 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
  • 15
    • 52649157711 scopus 로고    scopus 로고
    • Combined use of RNAi and quantitative proteomics to study gene function in drosophila
    • Bonaldi T, Straub T, Cox J et al (2008) Combined use of RNAi and quantitative proteomics to study gene function in Drosophila. Mol Cell 31:762-772
    • (2008) Mol. Cell. , vol.31 , pp. 762-772
    • Bonaldi, T.1    Straub, T.2    Cox, J.3
  • 16
    • 77954371891 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture SILAC applied to quantitative proteomics of bacillus subtilis
    • Sou fiB, Kumar C, Gnad F et al (2010) Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis . J Proteome Res 9:3638-3646
    • (2010) J. Proteome. Res. , vol.9 , pp. 3638-3646
    • Soufi, B.1    Kumar, C.2    Gnad, F.3
  • 17
    • 28644448658 scopus 로고    scopus 로고
    • Stable isotope labeling of arabidopsis thaliana cells and quantitative proteomics by mass spectrometry
    • Gruhler A, Schulze WX, Matthiesen R et al (2005) Stable isotope labeling of Arabidopsis thaliana cells and quantitative proteomics by mass spectrometry. Mol Cell Proteomics 4:1697-1709
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1697-1709
    • Gruhler, A.1    Schulze, W.X.2    Matthiesen, R.3
  • 18
    • 77958018495 scopus 로고    scopus 로고
    • The SILAC fl y allows for accurate protein quantification in vivo
    • Sury MD, Chen JX, Selbach M (2010) The SILAC fl y 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.X.2    Selbach, M.3
  • 19
    • 47549099572 scopus 로고    scopus 로고
    • SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function
    • Krüger M, Moser M, Ussar S et al (2008) SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function. Cell 134:353-364
    • (2008) Cell , vol.134 , pp. 353-364
    • Krüger, M.1    Moser, M.2    Ussar, S.3
  • 20
    • 0012351964 scopus 로고    scopus 로고
    • Properties of 13C-substituted arginine instable isotope labeling by amino acids in cell culture SILAC
    • Ong SE, Kratchmarova I, Mann M (2003) Properties of 13C-substituted arginine instable isotope labeling by amino acids in cell culture (SILAC). J Proteome Res 2:173-181
    • (2003) J. Proteome. Res. , vol.2 , pp. 173-181
    • Ong, S.E.1    Kratchmarova, I.2    Mann, M.3
  • 21
    • 52649167339 scopus 로고    scopus 로고
    • Prevention of amino acid conversion in SILAC experiments with embryonic stem cells
    • Bendall SC, Hughes C, Stewart MH et al (2008) Prevention of amino acid conversion in SILAC experiments with embryonic stem cells. Mol Cell Proteomics 7:1587-1597
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1587-1597
    • Bendall, S.C.1    Hughes, C.2    Stewart, M.H.3
  • 22
    • 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 CC, De Lima AF, Chen ZA et al (2010) 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) Mol. Cell. Proteomics , vol.9 , pp. 1567-1577
    • Bicho, C.C.1    De Lima, A.F.2    Chen, Z.A.3
  • 23
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometrybased proteomics turns quantitative
    • Ong SE, Mann M (2005) Mass spectrometrybased proteomics turns quantitative. Nat Chem Biol 1:252-262
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 24
    • 16344389629 scopus 로고    scopus 로고
    • Metabolic labeling of proteins for proteomics
    • Beynon RJ, Pratt JM (2005) Metabolic labeling of proteins for proteomics. Mol Cell Proteomics 4:857-872
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 857-872
    • Beynon, R.J.1    Pratt, J.M.2
  • 25
    • 60849098775 scopus 로고    scopus 로고
    • Temporal pro filing of the adipocyte proteome during differentiation using a five-plex SILAC based strategy
    • Molina H, Yang Y, Ruch T et al (2009) Temporal pro filing of the adipocyte proteome during differentiation using a five-plex SILAC based strategy. J Proteome Res 8:48-58
    • (2009) J. Proteome. Res. , vol.8 , pp. 48-58
    • Molina, H.1    Yang, Y.2    Ruch, T.3
  • 26
    • 79953701087 scopus 로고    scopus 로고
    • Andromeda: A peptide search engine integrated into the maxquant environment
    • Cox J, Neuhauser N, Michalski A, Scheltema RA et al (2011) Andromeda: A peptide search engine integrated into the MaxQuant environment. J Proteome Res 10:1794-1805
    • (2011) J. Proteome. Res. , vol.10 , pp. 1794-1805
    • Cox, J.1    Neuhauser, N.2    Michalski, A.3    Scheltema, R.A.4
  • 27
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture SILAC
    • Ong SE, 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.E.1    Mann, M.2
  • 28
    • 33750336592 scopus 로고    scopus 로고
    • Quantitative proteomics to study mitogen-activated protein kinases
    • Blagoev B, Mann M (2006) Quantitative proteomics to study mitogen-activated protein kinases. Methods 40:243-250
    • (2006) Methods , vol.40 , pp. 243-250
    • Blagoev, B.1    Mann, M.2
  • 29
    • 79952448233 scopus 로고    scopus 로고
    • Preventing arginine-to-proline conversion in a cell line independent manner during cell cultivation under SILAC conditions
    • Lößner C, Warnken U, Pscherer A, Schnölzer M (2011) Preventing arginine-to-proline conversion in a cell line independent manner during cell cultivation under SILAC conditions. Anal Biochem 412:123-125
    • (2011) Anal. Biochem. , vol.412 , pp. 123-125
    • Lößner, C.1    Warnken, U.2    Pscherer, A.3    Schnölzer, M.4
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 31
    • 57449099865 scopus 로고    scopus 로고
    • Maxquant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteomewide protein quantification
    • Cox J, Mann M (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteomewide protein quantification. Nat Biotechnol 26:1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 32
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the maxquant computational platform for SILAC-based quantitative proteomics
    • Cox J, Matic I, Hilger M et al (2009) A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat Protoc 4:698-705
    • (2009) Nat. Protoc. , vol.4 , pp. 698-705
    • Cox, J.1    Matic, I.2    Hilger, M.3
  • 33
    • 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 (2008) Absolute SILAC for accurate quantitation of proteins in complex mixtures down to the attomole level. J Proteome Res 7:1118-1130
    • (2008) J. Proteome. Res. , vol.7 , pp. 1118-1130
    • Hanke, S.1    Besir, H.2    Oesterhelt, D.3    Mann, M.4
  • 34
    • 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
  • 35
    • 60849097304 scopus 로고    scopus 로고
    • Turnover of the human proteome: Determination of protein intracellular stability by dynamic SILAC
    • Doherty MK, Hammond DE, Clague MJ et al (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
  • 36
    • 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
  • 37
    • 77952226764 scopus 로고    scopus 로고
    • Super-SILAC mix for quantitative proteomics of human tumor tissue
    • Geiger T, Cox J, Ostasiewicz P et al (2010) Super-SILAC mix for quantitative proteomics of human tumor tissue. Nat Methods 7: 383-385
    • (2010) Nat. Methods , vol.7 , pp. 383-385
    • Geiger, T.1    Cox, J.2    Ostasiewicz, P.3
  • 38
    • 77958481159 scopus 로고    scopus 로고
    • Nucleosome-interacting proteins regulated by DNA and histone methylation
    • Bartke T, Vermeulen M, Xhemalce B et al (2010) Nucleosome-interacting proteins regulated by DNA and histone methylation. Cell 143:470-484
    • (2010) Cell , vol.143 , pp. 470-484
    • Bartke, T.1    Vermeulen, M.2    Xhemalce, B.3
  • 39
    • 78049334902 scopus 로고    scopus 로고
    • Trans-SILAC: Sorting out the non-cellautonomous proteome
    • Rechavi O, Kalman M, Fang Y et al (2010) Trans-SILAC: Sorting out the non-cellautonomous proteome. Nat Methods 7: 923-927
    • (2010) Nat. Methods , vol.7 , pp. 923-927
    • Rechavi, O.1    Kalman, M.2    Fang, Y.3
  • 40
    • 0032873415 scopus 로고    scopus 로고
    • Three new dominant drug resistance cassettes for gene disruption in saccharomyces cerevisiae
    • Goldstein AL, McCusker JH (1999) Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae . Yeast 15:1541-1553
    • (1999) Yeast , vol.15 , pp. 1541-1553
    • Goldstein, A.L.1    McCusker, J.H.2
  • 41
    • 0032775010 scopus 로고    scopus 로고
    • Epitope tagging of yeast genes using a PCRbased strategy: More tags and improved practical routines
    • Knop M, Siegers K, Pereira G et al (1999) Epitope tagging of yeast genes using a PCRbased strategy: More tags and improved practical routines. Yeast 15:963-972
    • (1999) Yeast , vol.15 , pp. 963-972
    • Knop, M.1    Siegers, K.2    Pereira, G.3


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