메뉴 건너뛰기




Volumn 15, Issue 18, 2015, Pages 3175-3192

Quantitative proteomics using SILAC: Principles, applications, and developments

Author keywords

MS; Quantitative proteomics; SILAC; Super SILAC; Technology

Indexed keywords

AMINO ACID; STABLE ISOTOPE; STABLE ISOTOPE LABELED AMINO ACID; UNCLASSIFIED DRUG;

EID: 84941637169     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201500108     Document Type: Review
Times cited : (156)

References (217)
  • 1
    • 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. 2001, 19, 946-951.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 2
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross, P. L., Huang, Y. N., Marchese, J. N., Williamson, B. et al., Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell Proteomics 2004, 3, 1154-1169.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4
  • 3
    • 35648942133 scopus 로고    scopus 로고
    • 8-plex quantitation of changes in cerebrospinal fluid protein expression in subjects undergoing intravenous immunoglobulin treatment for Alzheimer's disease
    • Choe, L., D'Ascenzo, M., Relkin, N. R., Pappin, D. et al., 8-plex quantitation of changes in cerebrospinal fluid protein expression in subjects undergoing intravenous immunoglobulin treatment for Alzheimer's disease. Proteomics 2007, 7, 3651-3660.
    • (2007) Proteomics , vol.7 , pp. 3651-3660
    • Choe, L.1    D'Ascenzo, M.2    Relkin, N.R.3    Pappin, D.4
  • 4
    • 12444345515 scopus 로고    scopus 로고
    • Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS
    • Thompson, A., Schafer, J., Kuhn, K., Kienle, S. et al., Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS. Anal. Chem. 2003, 75, 1895-1904.
    • (2003) Anal. Chem. , vol.75 , pp. 1895-1904
    • Thompson, A.1    Schafer, J.2    Kuhn, K.3    Kienle, S.4
  • 5
    • 0348014635 scopus 로고    scopus 로고
    • Stable-isotope dimethyl labeling for quantitative proteomics
    • Hsu, J. L., Huang, S. Y., Chow, N. H., Chen, S. H., Stable-isotope dimethyl labeling for quantitative proteomics. Anal. Chem. 2003, 75, 6843-6852.
    • (2003) Anal. Chem. , vol.75 , pp. 6843-6852
    • Hsu, J.L.1    Huang, S.Y.2    Chow, N.H.3    Chen, S.H.4
  • 6
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • Boersema, P. J., Raijmakers, R., Lemeer, S., Mohammed, S., Heck, A. J., Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Nat. Protoc. 2009, 4, 484-494.
    • (2009) Nat. Protoc. , vol.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3    Mohammed, S.4    Heck, A.J.5
  • 7
    • 33846105280 scopus 로고    scopus 로고
    • Proteolytic 18O-labeling strategies for quantitative proteomics
    • Miyagi, M., Rao, K. C., Proteolytic 18O-labeling strategies for quantitative proteomics. Mass Spectrom. Rev. 2007, 26, 121-136.
    • (2007) Mass Spectrom. Rev. , vol.26 , pp. 121-136
    • Miyagi, M.1    Rao, K.C.2
  • 8
    • 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., Blagoev, B., Kratchmarova, I., Kristensen, D. B. et al., Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell Proteomics 2002, 1, 376-386.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4
  • 9
    • 0041706161 scopus 로고    scopus 로고
    • Metabolic labeling of C. elegans and D. melanogaster for quantitative proteomics
    • Krijgsveld, J., Ketting, R. F., Mahmoudi, T., Johansen, J. et al., Metabolic labeling of C. elegans and D. melanogaster for quantitative proteomics. Nat. Biotechnol. 2003, 21, 927-931.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 927-931
    • Krijgsveld, J.1    Ketting, R.F.2    Mahmoudi, T.3    Johansen, J.4
  • 10
    • 79551500036 scopus 로고    scopus 로고
    • Less label, more free: approaches in label-free quantitative mass spectrometry
    • Neilson, K. A., Ali, N. A., Muralidharan, S., Mirzaei, M. et al., Less label, more free: approaches in label-free quantitative mass spectrometry. Proteomics 2011, 11, 535-553.
    • (2011) Proteomics , vol.11 , pp. 535-553
    • Neilson, K.A.1    Ali, N.A.2    Muralidharan, S.3    Mirzaei, M.4
  • 12
    • 65249144498 scopus 로고    scopus 로고
    • Evaluation of the variation in sample preparation for comparative proteomics using stable isotope labeling by amino acids in cell culture
    • Zhang, G., Fenyo, D., Neubert, T. A., Evaluation of the variation in sample preparation for comparative proteomics using stable isotope labeling by amino acids in cell culture. J. Proteome Res. 2009, 8, 1285-1292.
    • (2009) J. Proteome Res. , vol.8 , pp. 1285-1292
    • Zhang, G.1    Fenyo, D.2    Neubert, T.A.3
  • 13
    • 84859620478 scopus 로고    scopus 로고
    • iTRAQ analysis of a cell culture model for malignant transformation, including comparison with 2D-PAGE and SILAC
    • Putz, S. M., Boehm, A. M., Stiewe, T., Sickmann, A., iTRAQ analysis of a cell culture model for malignant transformation, including comparison with 2D-PAGE and SILAC. J. Proteome Res. 2012, 11, 2140-2153.
    • (2012) J. Proteome Res. , vol.11 , pp. 2140-2153
    • Putz, S.M.1    Boehm, A.M.2    Stiewe, T.3    Sickmann, A.4
  • 14
    • 84914162421 scopus 로고    scopus 로고
    • Comparing SILAC- and stable isotope dimethyl-labeling approaches for quantitative proteomics
    • Lau, H. T., Suh, H. W., Golkowski, M., Ong, S. E., Comparing SILAC- and stable isotope dimethyl-labeling approaches for quantitative proteomics. J. Proteome Res. 2014, 13, 4164-4174.
    • (2014) J. Proteome Res. , vol.13 , pp. 4164-4174
    • Lau, H.T.1    Suh, H.W.2    Golkowski, M.3    Ong, S.E.4
  • 15
    • 84863230118 scopus 로고    scopus 로고
    • Systematic comparison of label-free, metabolic labeling, and isobaric chemical labeling for quantitative proteomics on LTQ Orbitrap Velos
    • Li, Z., Adams, R. M., Chourey, K., Hurst, G. B. et al., Systematic comparison of label-free, metabolic labeling, and isobaric chemical labeling for quantitative proteomics on LTQ Orbitrap Velos. J. Proteome Res. 2012, 11, 1582-1590.
    • (2012) J. Proteome Res. , vol.11 , pp. 1582-1590
    • Li, Z.1    Adams, R.M.2    Chourey, K.3    Hurst, G.B.4
  • 16
    • 84878796897 scopus 로고    scopus 로고
    • Dynamic adipocyte phosphoproteome reveals that Akt directly regulates mTORC2
    • Humphrey, S. J., Yang, G., Yang, P., Fazakerley, D. J. et al., Dynamic adipocyte phosphoproteome reveals that Akt directly regulates mTORC2. Cell Metab. 2013, 17, 1009-1020.
    • (2013) Cell Metab. , vol.17 , pp. 1009-1020
    • Humphrey, S.J.1    Yang, G.2    Yang, P.3    Fazakerley, D.J.4
  • 17
    • 79551663189 scopus 로고    scopus 로고
    • Use of stable isotope labeling by amino acids in cell culture as a spike-in standard in quantitative proteomics
    • Geiger, T., Wisniewski, J. R., Cox, J., Zanivan, S. et al., Use of stable isotope labeling by amino acids in cell culture as a spike-in standard in quantitative proteomics. Nat. Protoc. 2011, 6, 147-157.
    • (2011) Nat. Protoc. , vol.6 , pp. 147-157
    • Geiger, T.1    Wisniewski, J.R.2    Cox, J.3    Zanivan, S.4
  • 18
    • 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 2010, 7, 383-385.
    • (2010) Nat. Methods , vol.7 , pp. 383-385
    • Geiger, T.1    Cox, J.2    Ostasiewicz, P.3    Wisniewski, J.R.4    Mann, M.5
  • 19
    • 84865595374 scopus 로고    scopus 로고
    • The expanding field of SILAC
    • Ong, S. E., The expanding field of SILAC. Anal. Bioanal. Chem. 2012, 404, 967-976.
    • (2012) Anal. Bioanal. Chem. , vol.404 , pp. 967-976
    • Ong, S.E.1
  • 20
    • 84925883876 scopus 로고    scopus 로고
    • Fifteen years of stable isotope labeling by amino acids in cell culture (SILAC)
    • Mann, M., Fifteen years of stable isotope labeling by amino acids in cell culture (SILAC). Methods Mol. Biol. 2014, 1188, 1-7.
    • (2014) Methods Mol. Biol. , vol.1188 , pp. 1-7
    • Mann, M.1
  • 21
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann, M., Functional and quantitative proteomics using SILAC. Nat. Rev. Mol. Cell Biol. 2006, 7, 952-958.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 952-958
    • Mann, M.1
  • 22
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster, L. J., De Hoog, C. L., Mann, M., Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc. Natl. Acad. Sci. USA 2003, 100, 5813-5818.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 23
    • 4043141477 scopus 로고    scopus 로고
    • Quantitative cancer proteomics: stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research
    • Everley, P. A., Krijgsveld, J., Zetter, B. R., Gygi, S. P., Quantitative cancer proteomics: stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research. Mol. Cell Proteomics 2004, 3, 729-735.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 729-735
    • Everley, P.A.1    Krijgsveld, J.2    Zetter, B.R.3    Gygi, S.P.4
  • 24
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong, S. E., Mittler, G., Mann, M., Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nat. Methods 2004, 1, 119-126.
    • (2004) Nat. Methods , vol.1 , pp. 119-126
    • Ong, S.E.1    Mittler, G.2    Mann, M.3
  • 25
    • 0033926022 scopus 로고    scopus 로고
    • Single amino acid (arginine) restriction: growth and death of cultured HeLa and human diploid fibroblasts
    • Wheatley, D. N., Scott, L., Lamb, J., Smith, S., Single amino acid (arginine) restriction: growth and death of cultured HeLa and human diploid fibroblasts. Cell Physiol. Biochem. 2000, 10, 37-55.
    • (2000) Cell Physiol. Biochem. , vol.10 , pp. 37-55
    • Wheatley, D.N.1    Scott, L.2    Lamb, J.3    Smith, S.4
  • 26
    • 0012351964 scopus 로고    scopus 로고
    • Properties of 13C-substituted arginine in stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong, S. E., Kratchmarova, I., Mann, M., Properties of 13C-substituted arginine in stable isotope labeling by amino acids in cell culture (SILAC). J. Proteome Res. 2003, 2, 173-181.
    • (2003) J. Proteome Res. , vol.2 , pp. 173-181
    • Ong, S.E.1    Kratchmarova, I.2    Mann, M.3
  • 27
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics
    • Blagoev, B., Ong, S. E., Kratchmarova, I., Mann, M., Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics. Nat. Biotechnol. 2004, 22, 1139-1145.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.E.2    Kratchmarova, I.3    Mann, M.4
  • 29
    • 1942501808 scopus 로고    scopus 로고
    • A novel proteomic approach for specific identification of tyrosine kinase substrates using [13C] tyrosine
    • Ibarrola, N., Molina, H., Iwahori, A., Pandey, A., A novel proteomic approach for specific identification of tyrosine kinase substrates using [13C] tyrosine. J. Biol. Chem. 2004, 279, 15805-15813.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15805-15813
    • Ibarrola, N.1    Molina, H.2    Iwahori, A.3    Pandey, A.4
  • 30
    • 84885648123 scopus 로고    scopus 로고
    • Development of a 5-plex SILAC method tuned for the quantitation of tyrosine phosphorylation dynamics
    • Tzouros, M., Golling, S., Avila, D., Lamerz, J. et al., Development of a 5-plex SILAC method tuned for the quantitation of tyrosine phosphorylation dynamics. Mol. Cell Proteomics 2013, 12, 3339-3349.
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 3339-3349
    • Tzouros, M.1    Golling, S.2    Avila, D.3    Lamerz, J.4
  • 31
    • 0035499083 scopus 로고    scopus 로고
    • Fractionation of isotopically labeled peptides in quantitative proteomics
    • Zhang, R., Sioma, C. S., Wang, S., Regnier, F. E., Fractionation of isotopically labeled peptides in quantitative proteomics. Anal. Chem. 2001, 73, 5142-5149.
    • (2001) Anal. Chem. , vol.73 , pp. 5142-5149
    • Zhang, R.1    Sioma, C.S.2    Wang, S.3    Regnier, F.E.4
  • 32
    • 0036523809 scopus 로고    scopus 로고
    • Minimizing resolution of isotopically coded peptides in comparative proteomics
    • Zhang, R., Regnier, F. E., Minimizing resolution of isotopically coded peptides in comparative proteomics. J. Proteome Res. 2002, 1, 139-147.
    • (2002) J. Proteome Res. , vol.1 , pp. 139-147
    • Zhang, R.1    Regnier, F.E.2
  • 33
    • 3543121341 scopus 로고    scopus 로고
    • Quantification in proteomics through stable isotope coding: a review
    • Julka, S., Regnier, F., Quantification in proteomics through stable isotope coding: a review. J. Proteome Res. 2004, 3, 350-363.
    • (2004) J. Proteome Res. , vol.3 , pp. 350-363
    • Julka, S.1    Regnier, F.2
  • 34
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to arginine and lysine residues
    • Olsen, J. V., Ong, S. E., Mann, M., Trypsin cleaves exclusively C-terminal to arginine and lysine residues. Mol. Cell Proteomics 2004, 3, 608-614.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 608-614
    • Olsen, J.V.1    Ong, S.E.2    Mann, M.3
  • 35
    • 79952448233 scopus 로고    scopus 로고
    • Preventing arginine-to-proline conversion in a cell-line-independent manner during cell cultivation under stable isotope labeling by amino acids in cell culture (SILAC) conditions
    • Lossner, C., Warnken, U., Pscherer, A., Schnolzer, M., Preventing arginine-to-proline conversion in a cell-line-independent manner during cell cultivation under stable isotope labeling by amino acids in cell culture (SILAC) conditions. Anal. Biochem. 2011, 412, 123-125.
    • (2011) Anal. Biochem. , vol.412 , pp. 123-125
    • Lossner, C.1    Warnken, U.2    Pscherer, A.3    Schnolzer, M.4
  • 36
    • 52649167339 scopus 로고    scopus 로고
    • Prevention of amino acid conversion in SILAC experiments with embryonic stem cells
    • Bendall, S. C., Hughes, C., Stewart, M. H., Doble, B. et al., Prevention of amino acid conversion in SILAC experiments with embryonic stem cells. Mol. Cell Proteomics 2008, 7, 1587-1597.
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 1587-1597
    • Bendall, S.C.1    Hughes, C.2    Stewart, M.H.3    Doble, B.4
  • 37
    • 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. 2006, 1, 2650-2660.
    • (2006) Nat. Protoc. , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 38
    • 34548356772 scopus 로고    scopus 로고
    • An experimental correction for arginine-to-proline conversion artifacts in SILAC-based quantitative proteomics
    • Van Hoof, D., Pinkse, M. W., Oostwaard, D. W., Mummery, C. L. et al., An experimental correction for arginine-to-proline conversion artifacts in SILAC-based quantitative proteomics. Nat. Methods 2007, 4, 677-678.
    • (2007) Nat. Methods , vol.4 , pp. 677-678
    • Van Hoof, D.1    Pinkse, M.W.2    Oostwaard, D.W.3    Mummery, C.L.4
  • 39
    • 41549117597 scopus 로고    scopus 로고
    • A quantitative analysis software tool for mass spectrometry-based proteomics
    • Park, S. K., Venable, J. D., Xu, T., Yates, J. R. 3rd., A quantitative analysis software tool for mass spectrometry-based proteomics. Nat. Methods 2008, 5, 319-322.
    • (2008) Nat. Methods , vol.5 , pp. 319-322
    • Park, S.K.1    Venable, J.D.2    Xu, T.3    Yates, J.R.4
  • 40
    • 61449134247 scopus 로고    scopus 로고
    • A computational approach to correct arginine-to-proline conversion in quantitative proteomics
    • Park, S. K., Liao, L., Kim, J. Y., Yates, J. R. 3rd., A computational approach to correct arginine-to-proline conversion in quantitative proteomics. Nat. Methods 2009, 6, 184-185.
    • (2009) Nat. Methods , vol.6 , pp. 184-185
    • Park, S.K.1    Liao, L.2    Kim, J.Y.3    Yates, J.R.4
  • 41
    • 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., Mechanism of divergent growth factor effects in mesenchymal stem cell differentiation. Science 2005, 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
  • 42
    • 60849098775 scopus 로고    scopus 로고
    • Temporal profiling of the adipocyte proteome during differentiation using a five-plex SILAC based strategy
    • Molina, H., Yang, Y., Ruch, T., Kim, J. W. et al., Temporal profiling of the adipocyte proteome during differentiation using a five-plex SILAC based strategy. J. Proteome Res. 2009, 8, 48-58.
    • (2009) J. Proteome Res. , vol.8 , pp. 48-58
    • Molina, H.1    Yang, Y.2    Ruch, T.3    Kim, J.W.4
  • 43
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B. et al., Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127, 635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4
  • 44
    • 34249678458 scopus 로고    scopus 로고
    • Quantitative proteomic assessment of very early cellular signaling events
    • Dengjel, J., Akimov, V., Olsen, J. V., Bunkenborg, J. et al., Quantitative proteomic assessment of very early cellular signaling events. Nat. Biotechnol. 2007, 25, 566-568.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 566-568
    • Dengjel, J.1    Akimov, V.2    Olsen, J.V.3    Bunkenborg, J.4
  • 45
    • 7044229935 scopus 로고    scopus 로고
    • Evaluation of metabolic labeling for comparative proteomics in breast cancer cells
    • Gehrmann, M. L., Hathout, Y., Fenselau, C., Evaluation of metabolic labeling for comparative proteomics in breast cancer cells. J. Proteome Res. 2004, 3, 1063-1068.
    • (2004) J. Proteome Res. , vol.3 , pp. 1063-1068
    • Gehrmann, M.L.1    Hathout, Y.2    Fenselau, C.3
  • 46
    • 63049089189 scopus 로고    scopus 로고
    • Preliminary quantitative profile of differential protein expression between rat L6 myoblasts and myotubes by stable isotope labeling with amino acids in cell culture
    • Cui, Z., Chen, X., Lu, B., Park, S. K. et al., Preliminary quantitative profile of differential protein expression between rat L6 myoblasts and myotubes by stable isotope labeling with amino acids in cell culture. Proteomics 2009, 9, 1274-1292.
    • (2009) Proteomics , vol.9 , pp. 1274-1292
    • Cui, Z.1    Chen, X.2    Lu, B.3    Park, S.K.4
  • 47
    • 84897062624 scopus 로고    scopus 로고
    • CoreFlow: a computational platform for integration, analysis and modeling of complex biological data
    • Pasculescu, A., Schoof, E. M., Creixell, P., Zheng, Y. et al., CoreFlow: a computational platform for integration, analysis and modeling of complex biological data. J. Proteomics 2014, 100, 167-173.
    • (2014) J. Proteomics , vol.100 , pp. 167-173
    • Pasculescu, A.1    Schoof, E.M.2    Creixell, P.3    Zheng, Y.4
  • 48
    • 1642314524 scopus 로고    scopus 로고
    • A novel proteomic screen for peptide-protein interactions
    • Schulze, W. X., Mann, M., A novel proteomic screen for peptide-protein interactions. J. Biol. Chem. 2004, 279, 10756-10764.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10756-10764
    • Schulze, W.X.1    Mann, M.2
  • 49
    • 84862193068 scopus 로고    scopus 로고
    • Effective correction of experimental errors in quantitative proteomics using stable isotope labeling by amino acids in cell culture (SILAC)
    • Park, S. S., Wu, W. W., Zhou, Y., Shen, R. F. et al., Effective correction of experimental errors in quantitative proteomics using stable isotope labeling by amino acids in cell culture (SILAC). J. Proteomics 2012, 75, 3720-3732.
    • (2012) J. Proteomics , vol.75 , pp. 3720-3732
    • Park, S.S.1    Wu, W.W.2    Zhou, Y.3    Shen, R.F.4
  • 50
    • 75149144996 scopus 로고    scopus 로고
    • A dual pressure linear ion trap Orbitrap instrument with very high sequencing speed
    • Olsen, J. V., Schwartz, J. C., Griep-Raming, J., Nielsen, M. L. et al., A dual pressure linear ion trap Orbitrap instrument with very high sequencing speed. Mol. Cell Proteomics 2009, 8, 2759-2769.
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 2759-2769
    • Olsen, J.V.1    Schwartz, J.C.2    Griep-Raming, J.3    Nielsen, M.L.4
  • 51
    • 80052769923 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics using Q Exactive, a high-performance benchtop quadrupole Orbitrap mass spectrometer
    • M111011015
    • Michalski, A., Damoc, E., Hauschild, J. P., Lange, O. et al., Mass spectrometry-based proteomics using Q Exactive, a high-performance benchtop quadrupole Orbitrap mass spectrometer. Mol. Cell Proteomics 2011, 10, M111.011015.
    • (2011) Mol. Cell Proteomics , vol.10
    • Michalski, A.1    Damoc, E.2    Hauschild, J.P.3    Lange, O.4
  • 52
    • 84861800006 scopus 로고    scopus 로고
    • Optimized fast and sensitive acquisition methods for shotgun proteomics on a quadrupole orbitrap mass spectrometer
    • Kelstrup, C. D., Young, C., Lavallee, R., Nielsen, M. L., Olsen, J. V., Optimized fast and sensitive acquisition methods for shotgun proteomics on a quadrupole orbitrap mass spectrometer. J. Proteome Res. 2012, 11, 3487-3497.
    • (2012) J. Proteome Res. , vol.11 , pp. 3487-3497
    • Kelstrup, C.D.1    Young, C.2    Lavallee, R.3    Nielsen, M.L.4    Olsen, J.V.5
  • 53
    • 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. 2008, 26, 1367-1372.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 54
    • 84925884333 scopus 로고    scopus 로고
    • MaxQuant for in-depth analysis of large SILAC datasets
    • Tyanova, S., Mann, M., Cox, J., MaxQuant for in-depth analysis of large SILAC datasets. Methods Mol. Biol. 2014, 1188, 351-364.
    • (2014) Methods Mol. Biol. , vol.1188 , pp. 351-364
    • Tyanova, S.1    Mann, M.2    Cox, J.3
  • 55
    • 79952117670 scopus 로고    scopus 로고
    • Software pipeline and data analysis for MS/MS proteomics: the trans-proteomic pipeline
    • Keller, A., Shteynberg, D., Software pipeline and data analysis for MS/MS proteomics: the trans-proteomic pipeline. Methods Mol. Biol. 2010, 694, 169-189.
    • (2010) Methods Mol. Biol. , vol.694 , pp. 169-189
    • Keller, A.1    Shteynberg, D.2
  • 56
    • 84901797978 scopus 로고    scopus 로고
    • pQuant improves quantitation by keeping out interfering signals and evaluating the accuracy of calculated ratios
    • Liu, C., Song, C. Q., Yuan, Z. F., Fu, Y. et al., pQuant improves quantitation by keeping out interfering signals and evaluating the accuracy of calculated ratios. Anal. Chem. 2014, 86, 5286-5294.
    • (2014) Anal. Chem. , vol.86 , pp. 5286-5294
    • Liu, C.1    Song, C.Q.2    Yuan, Z.F.3    Fu, Y.4
  • 57
    • 77949582719 scopus 로고    scopus 로고
    • Census for proteome quantification
    • Chapter 13, Unit 13
    • Park, S. K., Yates, J. R. 3rd., Census for proteome quantification. Curr. Protoc. Bioinformatics 2010, Chapter 13, Unit 13, 12, 1-11.
    • (2010) Curr. Protoc. Bioinformatics , vol.12 , pp. 1-11
    • Park, S.K.1    Yates, J.R.3.2
  • 58
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: tool for the unification of biology. The Gene Ontology Consortium
    • Ashburner, M., Ball, C. A., Blake, J. A., Botstein, D. et al., Gene ontology: tool for the unification of biology. The Gene Ontology Consortium. Nat. Genet. 2000, 25, 25-29.
    • (2000) Nat. Genet. , vol.25 , pp. 25-29
    • Ashburner, M.1    Ball, C.A.2    Blake, J.A.3    Botstein, D.4
  • 60
    • 58149193234 scopus 로고    scopus 로고
    • STRING 8-a global view on proteins and their functional interactions in 630 organisms
    • Jensen, L. J., Kuhn, M., Stark, M., Chaffron, S. et al., STRING 8-a global view on proteins and their functional interactions in 630 organisms. Nucleic Acids Res. 2009, 37, D412-D416.
    • (2009) Nucleic Acids Res. , vol.37 , pp. D412-D416
    • Jensen, L.J.1    Kuhn, M.2    Stark, M.3    Chaffron, S.4
  • 61
    • 0038175144 scopus 로고    scopus 로고
    • GoMiner: a resource for biological interpretation of genomic and proteomic data
    • Zeeberg, B. R., Feng, W., Wang, G., Wang, M. D. et al., GoMiner: a resource for biological interpretation of genomic and proteomic data. Genome Biol. 2003, 4, R28.
    • (2003) Genome Biol. , vol.4 , pp. R28
    • Zeeberg, B.R.1    Feng, W.2    Wang, G.3    Wang, M.D.4
  • 62
    • 0242490780 scopus 로고    scopus 로고
    • Cytoscape: a software environment for integrated models of biomolecular interaction networks
    • Shannon, P., Markiel, A., Ozier, O., Baliga, N. S. et al., Cytoscape: a software environment for integrated models of biomolecular interaction networks. Genome Res. 2003, 13, 2498-2504.
    • (2003) Genome Res. , vol.13 , pp. 2498-2504
    • Shannon, P.1    Markiel, A.2    Ozier, O.3    Baliga, N.S.4
  • 63
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da, W., Sherman, B. T., Lempicki, R. A., Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 2009, 4, 44-57.
    • (2009) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 64
    • 67349208911 scopus 로고    scopus 로고
    • Bioinformatics analysis of mass spectrometry-based proteomics data sets
    • Kumar, C., Mann, M., Bioinformatics analysis of mass spectrometry-based proteomics data sets. FEBS Lett. 2009, 583, 1703-1712.
    • (2009) FEBS Lett. , vol.583 , pp. 1703-1712
    • Kumar, C.1    Mann, M.2
  • 65
    • 79959424627 scopus 로고    scopus 로고
    • Quantitative, high-resolution proteomics for data-driven systems biology
    • Cox, J., Mann, M., Quantitative, high-resolution proteomics for data-driven systems biology. Annu. Rev. Biochem. 2011, 80, 273-299.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 273-299
    • Cox, J.1    Mann, M.2
  • 66
    • 84866150007 scopus 로고    scopus 로고
    • Mass spectrometry based proteomics, background, status and future needs
    • Roepstorff, P., Mass spectrometry based proteomics, background, status and future needs. Protein Cell 2012, 3, 641-647.
    • (2012) Protein Cell , vol.3 , pp. 641-647
    • Roepstorff, P.1
  • 67
    • 78149373866 scopus 로고    scopus 로고
    • Quantitative proteomic analysis reveals the perturbation of multiple cellular pathways in jurkat-T cells induced by doxorubicin
    • Dong, X., Xiong, L., Jiang, X., Wang, Y., Quantitative proteomic analysis reveals the perturbation of multiple cellular pathways in jurkat-T cells induced by doxorubicin. J. Proteome Res. 2010, 9, 5943-5951.
    • (2010) J. Proteome Res. , vol.9 , pp. 5943-5951
    • Dong, X.1    Xiong, L.2    Jiang, X.3    Wang, Y.4
  • 68
    • 76149138039 scopus 로고    scopus 로고
    • Quantitative proteomic analysis reveals the perturbation of multiple cellular pathways in HL-60 cells induced by arsenite treatment
    • Xiong, L., Wang, Y., Quantitative proteomic analysis reveals the perturbation of multiple cellular pathways in HL-60 cells induced by arsenite treatment. J. Proteome Res. 2010, 9, 1129-1137.
    • (2010) J. Proteome Res. , vol.9 , pp. 1129-1137
    • Xiong, L.1    Wang, Y.2
  • 69
    • 84863799085 scopus 로고    scopus 로고
    • 5-Aza-2′-deoxycytidine induced growth inhibition of leukemia cells through modulating endogenous cholesterol biosynthesis
    • M111016915
    • Zhang, F., Dai, X., Wang, Y., 5-Aza-2′-deoxycytidine induced growth inhibition of leukemia cells through modulating endogenous cholesterol biosynthesis. Mol. Cell Proteomics 2012, 11, M111.016915.
    • (2012) Mol. Cell Proteomics , vol.11
    • Zhang, F.1    Dai, X.2    Wang, Y.3
  • 70
    • 84876541392 scopus 로고    scopus 로고
    • Direct proteomic quantification of the secretome of activated immune cells
    • Meissner, F., Scheltema, R. A., Mollenkopf, H. J., Mann, M., Direct proteomic quantification of the secretome of activated immune cells. Science 2013, 340, 475-478.
    • (2013) Science , vol.340 , pp. 475-478
    • Meissner, F.1    Scheltema, R.A.2    Mollenkopf, H.J.3    Mann, M.4
  • 71
    • 77955976922 scopus 로고    scopus 로고
    • The grand challenge to decipher the cancer proteome
    • Hanash, S., Taguchi, A., The grand challenge to decipher the cancer proteome. Nat. Rev. Cancer 2010, 10, 652-660.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 652-660
    • Hanash, S.1    Taguchi, A.2
  • 72
    • 41649100689 scopus 로고    scopus 로고
    • Mining the plasma proteome for cancer biomarkers
    • Hanash, S. M., Pitteri, S. J., Faca, V. M., Mining the plasma proteome for cancer biomarkers. Nature 2008, 452, 571-579.
    • (2008) Nature , vol.452 , pp. 571-579
    • Hanash, S.M.1    Pitteri, S.J.2    Faca, V.M.3
  • 74
    • 31644434206 scopus 로고    scopus 로고
    • Biomarker discovery from pancreatic cancer secretome using a differential proteomic approach
    • Gronborg, M., Kristiansen, T. Z., Iwahori, A., Chang, R. et al., Biomarker discovery from pancreatic cancer secretome using a differential proteomic approach. Mol. Cell Proteomics 2006, 5, 157-171.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 157-171
    • Gronborg, M.1    Kristiansen, T.Z.2    Iwahori, A.3    Chang, R.4
  • 75
    • 78049240516 scopus 로고    scopus 로고
    • SILAC-based quantitative proteomic approach to identify potential biomarkers from the esophageal squamous cell carcinoma secretome
    • Kashyap, M. K., Harsha, H. C., Renuse, S., Pawar, H. et al., SILAC-based quantitative proteomic approach to identify potential biomarkers from the esophageal squamous cell carcinoma secretome. Cancer Biol. Ther. 2010, 10, 796-810.
    • (2010) Cancer Biol. Ther. , vol.10 , pp. 796-810
    • Kashyap, M.K.1    Harsha, H.C.2    Renuse, S.3    Pawar, H.4
  • 77
    • 84878724168 scopus 로고    scopus 로고
    • In-depth characterization of the secretome of colorectal cancer metastatic cells identifies key proteins in cell adhesion, migration, and invasion
    • Barderas, R., Mendes, M., Torres, S., Bartolome, R. A. et al., In-depth characterization of the secretome of colorectal cancer metastatic cells identifies key proteins in cell adhesion, migration, and invasion. Mol. Cell Proteomics 2013, 12, 1602-1620.
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 1602-1620
    • Barderas, R.1    Mendes, M.2    Torres, S.3    Bartolome, R.A.4
  • 78
    • 33750140109 scopus 로고    scopus 로고
    • Quantification of membrane and membrane-bound proteins in normal and malignant breast cancer cells isolated from the same patient with primary breast carcinoma
    • Liang, X., Zhao, J., Hajivandi, M., Wu, R. et al., Quantification of membrane and membrane-bound proteins in normal and malignant breast cancer cells isolated from the same patient with primary breast carcinoma. J. Proteome Res. 2006, 5, 2632-2641.
    • (2006) J. Proteome Res. , vol.5 , pp. 2632-2641
    • Liang, X.1    Zhao, J.2    Hajivandi, M.3    Wu, R.4
  • 79
    • 67049098536 scopus 로고    scopus 로고
    • Efficient isolation and quantitative proteomic analysis of cancer cell plasma membrane proteins for identification of metastasis-associated cell surface markers
    • Lund, R., Leth-Larsen, R., Jensen, O. N., Ditzel, H. J., Efficient isolation and quantitative proteomic analysis of cancer cell plasma membrane proteins for identification of metastasis-associated cell surface markers. J. Proteome Res. 2009, 8, 3078-3090.
    • (2009) J. Proteome Res. , vol.8 , pp. 3078-3090
    • Lund, R.1    Leth-Larsen, R.2    Jensen, O.N.3    Ditzel, H.J.4
  • 80
    • 67049095042 scopus 로고    scopus 로고
    • Metastasis-related plasma membrane proteins of human breast cancer cells identified by comparative quantitative mass spectrometry
    • Leth-Larsen, R., Lund, R., Hansen, H. V., Laenkholm, A. V. et al., Metastasis-related plasma membrane proteins of human breast cancer cells identified by comparative quantitative mass spectrometry. Mol. Cell Proteomics 2009, 8, 1436-1449.
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 1436-1449
    • Leth-Larsen, R.1    Lund, R.2    Hansen, H.V.3    Laenkholm, A.V.4
  • 81
    • 77649115961 scopus 로고    scopus 로고
    • Differential protein expression on the cell surface of colorectal cancer cells associated to tumor metastasis
    • Luque-Garcia, J. L., Martinez-Torrecuadrada, J. L., Epifano, C., Canamero, M. et al., Differential protein expression on the cell surface of colorectal cancer cells associated to tumor metastasis. Proteomics 2010, 10, 940-952.
    • (2010) Proteomics , vol.10 , pp. 940-952
    • Luque-Garcia, J.L.1    Martinez-Torrecuadrada, J.L.2    Epifano, C.3    Canamero, M.4
  • 82
    • 33745608428 scopus 로고    scopus 로고
    • Systematic characterization of nuclear proteome during apoptosis: a quantitative proteomic study by differential extraction and stable isotope labeling
    • Hwang, S. I., Lundgren, D. H., Mayya, V., Rezaul, K. et al., Systematic characterization of nuclear proteome during apoptosis: a quantitative proteomic study by differential extraction and stable isotope labeling. Mol. Cell Proteomics 2006, 5, 1131-1145.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 1131-1145
    • Hwang, S.I.1    Lundgren, D.H.2    Mayya, V.3    Rezaul, K.4
  • 83
    • 67649135074 scopus 로고    scopus 로고
    • Temporal and spatial profiling of nuclei-associated proteins upon TNF-alpha/NF-kappaB signaling
    • Ma, D. J., Li, S. J., Wang, L. S., Dai, J. et al., Temporal and spatial profiling of nuclei-associated proteins upon TNF-alpha/NF-kappaB signaling. Cell Res. 2009, 19, 651-664.
    • (2009) Cell Res. , vol.19 , pp. 651-664
    • Ma, D.J.1    Li, S.J.2    Wang, L.S.3    Dai, J.4
  • 84
    • 77957355995 scopus 로고    scopus 로고
    • Quantitative proteomics using SILAC coupled to LC-MS/MS reveals changes in the nucleolar proteome in influenza A virus-infected cells
    • Emmott, E., Wise, H., Loucaides, E. M., Matthews, D. A. et al., Quantitative proteomics using SILAC coupled to LC-MS/MS reveals changes in the nucleolar proteome in influenza A virus-infected cells. J. Proteome Res. 2010, 9, 5335-5345.
    • (2010) J. Proteome Res. , vol.9 , pp. 5335-5345
    • Emmott, E.1    Wise, H.2    Loucaides, E.M.3    Matthews, D.A.4
  • 85
    • 84864815790 scopus 로고    scopus 로고
    • Modulation of neuronal pentraxin 1 expression in rat pancreatic beta-cells submitted to chronic glucotoxic stress
    • Schvartz, D., Coute, Y., Brunner, Y., Wollheim, C. B., Sanchez, J. C., Modulation of neuronal pentraxin 1 expression in rat pancreatic beta-cells submitted to chronic glucotoxic stress. Mol. Cell Proteomics 2012, 11, 244-254.
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 244-254
    • Schvartz, D.1    Coute, Y.2    Brunner, Y.3    Wollheim, C.B.4    Sanchez, J.C.5
  • 86
    • 77953589749 scopus 로고    scopus 로고
    • Mammalian mitochondrial proteomics: insights into mitochondrial functions and mitochondria-related diseases
    • Chen, X., Li, J., Hou, J., Xie, Z., Yang, F., Mammalian mitochondrial proteomics: insights into mitochondrial functions and mitochondria-related diseases. Expert Rev. Proteomics 2010, 7, 333-345.
    • (2010) Expert Rev. Proteomics , vol.7 , pp. 333-345
    • Chen, X.1    Li, J.2    Hou, J.3    Xie, Z.4    Yang, F.5
  • 87
    • 84885392656 scopus 로고    scopus 로고
    • Chronic high glucose induced INS-1beta cell mitochondrial dysfunction: a comparative mitochondrial proteome with SILAC
    • Chen, X., Cui, Z., Wei, S., Hou, J. et al., Chronic high glucose induced INS-1beta cell mitochondrial dysfunction: a comparative mitochondrial proteome with SILAC. Proteomics 2013, 13, 3030-3039.
    • (2013) Proteomics , vol.13 , pp. 3030-3039
    • Chen, X.1    Cui, Z.2    Wei, S.3    Hou, J.4
  • 88
    • 84907509266 scopus 로고    scopus 로고
    • Quantitative proteomics analysis identifies mitochondria as therapeutic targets of multidrug-resistance in ovarian cancer
    • Chen, X., Wei, S., Ma, Y., Lu, J. et al., Quantitative proteomics analysis identifies mitochondria as therapeutic targets of multidrug-resistance in ovarian cancer. Theranostics 2014, 4, 1164-1175.
    • (2014) Theranostics , vol.4 , pp. 1164-1175
    • Chen, X.1    Wei, S.2    Ma, Y.3    Lu, J.4
  • 89
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann, M., Jensen, O. N., Proteomic analysis of post-translational modifications. Nat. Biotechnol. 2003, 21, 255-261.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 90
    • 65249137629 scopus 로고    scopus 로고
    • Global and site-specific quantitative phosphoproteomics: principles and applications
    • Macek, B., Mann, M., Olsen, J. V., Global and site-specific quantitative phosphoproteomics: principles and applications. Annu. Rev. Pharmacol. Toxicol. 2009, 49, 199-221.
    • (2009) Annu. Rev. Pharmacol. Toxicol. , vol.49 , pp. 199-221
    • Macek, B.1    Mann, M.2    Olsen, J.V.3
  • 91
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome
    • Mann, M., Ong, S. E., Gronborg, M., Steen, H. et al., Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol. 2002, 20, 261-268.
    • (2002) Trends Biotechnol. , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.E.2    Gronborg, M.3    Steen, H.4
  • 92
    • 34250878954 scopus 로고    scopus 로고
    • Mechanisms of specificity in protein phosphorylation
    • Ubersax, J. A., Ferrell, J. E., Jr., Mechanisms of specificity in protein phosphorylation. Nat. Rev. Mol. Cell Biol. 2007, 8, 530-541.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 530-541
    • Ubersax, J.A.1    Ferrell Jr, J.E.2
  • 93
    • 79952752375 scopus 로고    scopus 로고
    • System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation
    • Rigbolt, K. T., Prokhorova, T. A., Akimov, V., Henningsen, J. et al., System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci. Signal. 2011, 4, rs3.
    • (2011) Sci. Signal. , vol.4 , pp. rs3
    • Rigbolt, K.T.1    Prokhorova, T.A.2    Akimov, V.3    Henningsen, J.4
  • 94
    • 63049113651 scopus 로고    scopus 로고
    • Analytical strategies for phosphoproteomics
    • Thingholm, T. E., Jensen, O. N., Larsen, M. R., Analytical strategies for phosphoproteomics. Proteomics 2009, 9, 1451-1468.
    • (2009) Proteomics , vol.9 , pp. 1451-1468
    • Thingholm, T.E.1    Jensen, O.N.2    Larsen, M.R.3
  • 95
    • 26844529338 scopus 로고    scopus 로고
    • Enrichment of phosphoproteins for proteomic analysis using immobilized Fe(III)-affinity adsorption chromatography
    • Guerrera, I. C., Predic-Atkinson, J., Kleiner, O., Soskic, V., Godovac-Zimmermann, J., Enrichment of phosphoproteins for proteomic analysis using immobilized Fe(III)-affinity adsorption chromatography. J. Proteome Res. 2005, 4, 1545-1553.
    • (2005) J. Proteome Res. , vol.4 , pp. 1545-1553
    • Guerrera, I.C.1    Predic-Atkinson, J.2    Kleiner, O.3    Soskic, V.4    Godovac-Zimmermann, J.5
  • 96
    • 84867041794 scopus 로고    scopus 로고
    • Advances in phosphopeptide enrichment techniques for phosphoproteomics
    • Beltran, L., Cutillas, P. R., Advances in phosphopeptide enrichment techniques for phosphoproteomics. Amino Acids 2012, 43, 1009-1024.
    • (2012) Amino Acids , vol.43 , pp. 1009-1024
    • Beltran, L.1    Cutillas, P.R.2
  • 97
    • 0036198435 scopus 로고    scopus 로고
    • Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae
    • Ficarro, S. B., McCleland, M. L., Stukenberg, P. T., Burke, D. J. et al., Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae. Nat. Biotechnol. 2002, 20, 301-305.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 301-305
    • Ficarro, S.B.1    McCleland, M.L.2    Stukenberg, P.T.3    Burke, D.J.4
  • 98
    • 65349130025 scopus 로고    scopus 로고
    • Enrichment and characterization of phosphopeptides by immobilized metal affinity chromatography (IMAC) and mass spectrometry
    • xi.
    • Thingholm, T. E., Jensen, O. N., Enrichment and characterization of phosphopeptides by immobilized metal affinity chromatography (IMAC) and mass spectrometry. Methods Mol. Biol. 2009, 527, 47-56, xi.
    • (2009) Methods Mol. Biol. , vol.527 , pp. 47-56
    • Thingholm, T.E.1    Jensen, O.N.2
  • 99
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen, M. R., Thingholm, T. E., Jensen, O. N., Roepstorff, P., Jorgensen, T. J., Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell Proteomics 2005, 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    Jorgensen, T.J.5
  • 100
    • 38049035341 scopus 로고    scopus 로고
    • Global profiling of phosphopeptides by titania affinity enrichment
    • Wu, J., Shakey, Q., Liu, W., Schuller, A., Follettie, M. T., Global profiling of phosphopeptides by titania affinity enrichment. J. Proteome Res. 2007, 6, 4684-4689.
    • (2007) J. Proteome Res. , vol.6 , pp. 4684-4689
    • Wu, J.1    Shakey, Q.2    Liu, W.3    Schuller, A.4    Follettie, M.T.5
  • 102
    • 43849091451 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection
    • McNulty, D. E., Annan, R. S., Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection. Mol. Cell Proteomics 2008, 7, 971-980.
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 971-980
    • McNulty, D.E.1    Annan, R.S.2
  • 103
    • 79961217471 scopus 로고    scopus 로고
    • Comparison of ERLIC-TiO2, HILIC-TiO2, and SCX-TiO2 for global phosphoproteomics approaches
    • Zarei, M., Sprenger, A., Metzger, F., Gretzmeier, C., Dengjel, J., Comparison of ERLIC-TiO2, HILIC-TiO2, and SCX-TiO2 for global phosphoproteomics approaches. J. Proteome Res. 2011, 10, 3474-3483.
    • (2011) J. Proteome Res. , vol.10 , pp. 3474-3483
    • Zarei, M.1    Sprenger, A.2    Metzger, F.3    Gretzmeier, C.4    Dengjel, J.5
  • 104
    • 15944377809 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway
    • Gruhler, A., Olsen, J. V., Mohammed, S., Mortensen, P. et al., Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway. Mol. Cell Proteomics 2005, 4, 310-327.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 310-327
    • Gruhler, A.1    Olsen, J.V.2    Mohammed, S.3    Mortensen, P.4
  • 105
    • 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., Comparative phosphoproteomics studies of macrophage response to bacterial virulence effectors. J. Proteomics 2012, 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
  • 106
    • 84859562238 scopus 로고    scopus 로고
    • Global analysis of phosphoproteome regulation by the Ser/Thr phosphatase Ppt1 in Saccharomyces cerevisiae
    • Schreiber, T. B., Mausbacher, N., Soroka, J., Wandinger, S. K. et al., Global analysis of phosphoproteome regulation by the Ser/Thr phosphatase Ppt1 in Saccharomyces cerevisiae. J. Proteome Res. 2012, 11, 2397-2408.
    • (2012) J. Proteome Res. , vol.11 , pp. 2397-2408
    • Schreiber, T.B.1    Mausbacher, N.2    Soroka, J.3    Wandinger, S.K.4
  • 107
    • 77953148666 scopus 로고    scopus 로고
    • Site-specific phosphorylation dynamics of the nuclear proteome during the DNA damage response
    • Bennetzen, M. V., Larsen, D. H., Bunkenborg, J., Bartek, J. et al., Site-specific phosphorylation dynamics of the nuclear proteome during the DNA damage response. Mol. Cell Proteomics 2010, 9, 1314-1323.
    • (2010) Mol. Cell Proteomics , vol.9 , pp. 1314-1323
    • Bennetzen, M.V.1    Larsen, D.H.2    Bunkenborg, J.3    Bartek, J.4
  • 108
    • 72449196261 scopus 로고    scopus 로고
    • Global effects of kinase inhibitors on signaling networks revealed by quantitative phosphoproteomics
    • Pan, C., Olsen, J. V., Daub, H., Mann, M., Global effects of kinase inhibitors on signaling networks revealed by quantitative phosphoproteomics. Mol. Cell. Proteomics 2009, 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
  • 109
    • 70349621112 scopus 로고    scopus 로고
    • Systems-wide analysis of a phosphatase knock-down by quantitative proteomics and phosphoproteomics
    • Hilger, M., Bonaldi, T., Gnad, F., Mann, M., Systems-wide analysis of a phosphatase knock-down by quantitative proteomics and phosphoproteomics. Mol. Cell. Proteomics 2009, 8, 1908-1920.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1908-1920
    • Hilger, M.1    Bonaldi, T.2    Gnad, F.3    Mann, M.4
  • 110
    • 84921569189 scopus 로고    scopus 로고
    • Activation of diverse signalling pathways by oncogenic PIK3CA mutations
    • Wu, X., Renuse, S., Sahasrabuddhe, N. A., Zahari, M. S. et al., Activation of diverse signalling pathways by oncogenic PIK3CA mutations. Nat. Commun. 2014, 5, 4961.
    • (2014) Nat. Commun. , vol.5 , pp. 4961
    • Wu, X.1    Renuse, S.2    Sahasrabuddhe, N.A.3    Zahari, M.S.4
  • 111
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush, J., Moritz, A., Lee, K. A., Guo, A. et al., Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat. Biotechnol. 2005, 23, 94-101.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 94-101
    • Rush, J.1    Moritz, A.2    Lee, K.A.3    Guo, A.4
  • 112
    • 36849065315 scopus 로고    scopus 로고
    • Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer
    • Rikova, K., Guo, A., Zeng, Q., Possemato, A. et al., Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell 2007, 131, 1190-1203.
    • (2007) Cell , vol.131 , pp. 1190-1203
    • Rikova, K.1    Guo, A.2    Zeng, Q.3    Possemato, A.4
  • 113
    • 82755163975 scopus 로고    scopus 로고
    • Comparison of three quantitative phosphoproteomic strategies to study receptor tyrosine kinase signaling
    • Zhang, G., Neubert, T. A., Comparison of three quantitative phosphoproteomic strategies to study receptor tyrosine kinase signaling. J. Proteome Res. 2011, 10, 5454-5462.
    • (2011) J. Proteome Res. , vol.10 , pp. 5454-5462
    • Zhang, G.1    Neubert, T.A.2
  • 114
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L. et al., Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 2009, 325, 834-840.
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4
  • 115
    • 84878524313 scopus 로고    scopus 로고
    • Acetylation dynamics of human nuclear proteins during the ionizing radiation-induced DNA damage response
    • Bennetzen, M. V., Larsen, D. H., Dinant, C., Watanabe, S. et al., Acetylation dynamics of human nuclear proteins during the ionizing radiation-induced DNA damage response. Cell Cycle 2013, 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
  • 116
    • 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. et al., SAHA treatment reveals the link between histone lysine acetylation and proteome in nonsmall cell lung cancer A549 Cells. J. Proteome Res. 2013, 12, 4064-4073.
    • (2013) J. Proteome Res. , vol.12 , pp. 4064-4073
    • Wu, Q.1    Xu, W.2    Cao, L.3    Li, X.4
  • 117
    • 34548438595 scopus 로고    scopus 로고
    • Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation
    • Wang, Z., Pandey, A., Hart, G. W., Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation. Mol. Cell. Proteomics 2007, 6, 1365-1379.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1365-1379
    • Wang, Z.1    Pandey, A.2    Hart, G.W.3
  • 118
    • 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, D. F., Mann, M., Wisniewski, J. R., Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry. J. Proteome Res. 2010, 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
  • 119
    • 84871860708 scopus 로고    scopus 로고
    • Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples
    • Boersema, P. J., Geiger, T., Wisniewski, J. R., Mann, M., Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples. Mol. Cell Proteomics 2013, 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
  • 120
    • 55949136614 scopus 로고    scopus 로고
    • Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry
    • Meierhofer, D., Wang, X., Huang, L., Kaiser, P., Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J. Proteome Res. 2008, 7, 4566-4576.
    • (2008) J. Proteome Res. , vol.7 , pp. 4566-4576
    • Meierhofer, D.1    Wang, X.2    Huang, L.3    Kaiser, P.4
  • 121
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D. et al., Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 2009, 137, 133-145.
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.4
  • 122
    • 80755175389 scopus 로고    scopus 로고
    • Characterization of ubiquitination dependent dynamics in growth factor receptor signaling by quantitative proteomics
    • Akimov, V., Rigbolt, K. T., Nielsen, M. M., Blagoev, B., Characterization of ubiquitination dependent dynamics in growth factor receptor signaling by quantitative proteomics. Mol. Biosyst. 2011, 7, 3223-3233.
    • (2011) Mol. Biosyst. , vol.7 , pp. 3223-3233
    • Akimov, V.1    Rigbolt, K.T.2    Nielsen, M.M.3    Blagoev, B.4
  • 123
    • 77449086407 scopus 로고    scopus 로고
    • In vivo residue-specific histone methylation dynamics
    • Zee, B. M., Levin, R. S., Xu, B., LeRoy, G. et al., In vivo residue-specific histone methylation dynamics. J. Biol. Chem. 2009, 285, 3341-3350.
    • (2009) J. Biol. Chem. , vol.285 , pp. 3341-3350
    • Zee, B.M.1    Levin, R.S.2    Xu, B.3    LeRoy, G.4
  • 124
    • 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. J., Zee, B. M., Garcia, B. A., 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. 2013, 977, 299-313.
    • (2013) Methods Mol. Biol. , vol.977 , pp. 299-313
    • Cao, X.J.1    Zee, B.M.2    Garcia, B.A.3
  • 126
    • 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. et al., Analysis of dynamic changes in post-translational modifications of human histones during cell cycle by mass spectrometry. Mol. Cell. Proteomics 2007, 6, 1917-1932.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1917-1932
    • Bonenfant, D.1    Towbin, H.2    Coulot, M.3    Schindler, P.4
  • 127
    • 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., SILAC-based proteomic analysis to dissect the "histone modification signature" of human breast cancer cells. Amino Acids 2010, 41, 387-399.
    • (2010) Amino Acids , vol.41 , pp. 387-399
    • Cuomo, A.1    Moretti, S.2    Minucci, S.3    Bonaldi, T.4
  • 128
    • 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, M. R., Freitas, M. A., Discovery of histone modification crosstalk networks by stable isotope labeling of amino acids in cell culture mass spectrometry (SILAC MS). Mol. Cell. Proteomics 2013, 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
  • 129
    • 84921282104 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics reveals crosstalk between phosphorylation and O-GlcNAc in the DNA damage response pathway
    • Zhong, J., Martinez, M., Sengupta, S., Lee, A. et al., Quantitative phosphoproteomics reveals crosstalk between phosphorylation and O-GlcNAc in the DNA damage response pathway. Proteomics 2015, 15, 591-607.
    • (2015) Proteomics , vol.15 , pp. 591-607
    • Zhong, J.1    Martinez, M.2    Sengupta, S.3    Lee, A.4
  • 130
    • 84890641204 scopus 로고    scopus 로고
    • The coming of age of phosphoproteomics-from large data sets to inference of protein functions
    • Roux, P. P., Thibault, P., The coming of age of phosphoproteomics-from large data sets to inference of protein functions. Mol. Cell. Proteomics 2013, 12, 3453-3464.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 3453-3464
    • Roux, P.P.1    Thibault, P.2
  • 131
    • 84873991171 scopus 로고    scopus 로고
    • Investigation of stable and transient protein-protein interactions: past, present, and future
    • Ngounou Wetie, A. G., Sokolowska, I., Woods, A. G., Roy, U. et al., Investigation of stable and transient protein-protein interactions: past, present, and future. Proteomics 2012, 13, 538-557.
    • (2012) Proteomics , vol.13 , pp. 538-557
    • Ngounou Wetie, A.G.1    Sokolowska, I.2    Woods, A.G.3    Roy, U.4
  • 132
    • 49549121813 scopus 로고    scopus 로고
    • High confidence determination of specific protein-protein interactions using quantitative mass spectrometry
    • Vermeulen, M., Hubner, N. C., Mann, M., High confidence determination of specific protein-protein interactions using quantitative mass spectrometry. Curr. Opin. Biotechnol. 2008, 19, 331-337.
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 331-337
    • Vermeulen, M.1    Hubner, N.C.2    Mann, M.3
  • 133
    • 33751211249 scopus 로고    scopus 로고
    • An efficient tandem affinity purification procedure for interaction proteomics in mammalian cells
    • Burckstummer, T., Bennett, K. L., Preradovic, A., Schutze, G. et al., An efficient tandem affinity purification procedure for interaction proteomics in mammalian cells. Nat. Methods 2006, 3, 1013-1019.
    • (2006) Nat. Methods , vol.3 , pp. 1013-1019
    • Burckstummer, T.1    Bennett, K.L.2    Preradovic, A.3    Schutze, G.4
  • 134
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz, P., Giot, L., Cagney, G., Mansfield, T. A. et al., A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 2000, 403, 623-627.
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1    Giot, L.2    Cagney, G.3    Mansfield, T.A.4
  • 135
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho, Y., Gruhler, A., Heilbut, A., Bader, G. D. et al., Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 2002, 415, 180-183.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3    Bader, G.D.4
  • 136
    • 79959211995 scopus 로고    scopus 로고
    • Analyzing protein-protein interactions by quantitative mass spectrometry
    • Paul, F. E., Hosp, F., Selbach, M., Analyzing protein-protein interactions by quantitative mass spectrometry. Methods 2011, 54, 387-395.
    • (2011) Methods , vol.54 , pp. 387-395
    • Paul, F.E.1    Hosp, F.2    Selbach, M.3
  • 137
    • 55949116385 scopus 로고    scopus 로고
    • Identifying specific protein interaction partners using quantitative mass spectrometry and bead proteomes
    • Trinkle-Mulcahy, L., Boulon, S., Lam, Y. W., Urcia, R. et al., Identifying specific protein interaction partners using quantitative mass spectrometry and bead proteomes. J. Cell Biol. 2008, 183, 223-239.
    • (2008) J. Cell Biol. , vol.183 , pp. 223-239
    • Trinkle-Mulcahy, L.1    Boulon, S.2    Lam, Y.W.3    Urcia, R.4
  • 138
    • 84907424304 scopus 로고    scopus 로고
    • A mass spectrometry view of stable and transient protein interactions
    • Budayeva, H. G., Cristea, I. M., A mass spectrometry view of stable and transient protein interactions. Adv. Exp. Med. Biol. 2014, 806, 263-282.
    • (2014) Adv. Exp. Med. Biol. , vol.806 , pp. 263-282
    • Budayeva, H.G.1    Cristea, I.M.2
  • 139
    • 0037370399 scopus 로고    scopus 로고
    • The study of macromolecular complexes by quantitative proteomics
    • Ranish, J. A., Yi, E. C., Leslie, D. M., Purvine, S. O. et al., The study of macromolecular complexes by quantitative proteomics. Nat. Genet. 2003, 33, 349-355.
    • (2003) Nat. Genet. , vol.33 , pp. 349-355
    • Ranish, J.A.1    Yi, E.C.2    Leslie, D.M.3    Purvine, S.O.4
  • 140
    • 0038371369 scopus 로고    scopus 로고
    • Quantitative chemical proteomics for identifying candidate drug targets
    • Oda, Y., Owa, T., Sato, T., Boucher, B. et al., Quantitative chemical proteomics for identifying candidate drug targets. Anal. Chem. 2003, 75, 2159-2165.
    • (2003) Anal. Chem. , vol.75 , pp. 2159-2165
    • Oda, Y.1    Owa, T.2    Sato, T.3    Boucher, B.4
  • 141
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev, B., Kratchmarova, I., Ong, S. E., Nielsen, M. et al., A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat. Biotechnol. 2003, 21, 315-318.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4
  • 142
    • 26844556166 scopus 로고    scopus 로고
    • I-DIRT, a general method for distinguishing between specific and nonspecific protein interactions
    • Tackett, A. J., DeGrasse, J. A., Sekedat, M. D., Oeffinger, M. et al., I-DIRT, a general method for distinguishing between specific and nonspecific protein interactions. J. Proteome Res. 2005, 4, 1752-1756.
    • (2005) J. Proteome Res. , vol.4 , pp. 1752-1756
    • Tackett, A.J.1    DeGrasse, J.A.2    Sekedat, M.D.3    Oeffinger, M.4
  • 143
    • 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. et al., The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC. J. Proteomics 2010, 74, 294-303.
    • (2010) J. Proteomics , vol.74 , pp. 294-303
    • Zhong, J.1    Chaerkady, R.2    Kandasamy, K.3    Gucek, M.4
  • 144
    • 40849108777 scopus 로고    scopus 로고
    • Mapping the integrin-linked kinase interactome using SILAC
    • Dobreva, I., Fielding, A., Foster, L. J., Dedhar, S., Mapping the integrin-linked kinase interactome using SILAC. J. Proteome Res. 2008, 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
  • 145
    • 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, L. J., Rudich, A., Talior, I., Patel, N. et al., Insulin-dependent interactions of proteins with GLUT4 revealed through stable isotope labeling by amino acids in cell culture (SILAC). J. Proteome Res. 2006, 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
  • 146
    • 84925884050 scopus 로고    scopus 로고
    • SILAC labeling of yeast for the study of membrane protein complexes
    • Oeljeklaus, S., Schummer, A., Suppanz, I., Warscheid, B., SILAC labeling of yeast for the study of membrane protein complexes. Methods Mol. Biol. 2014, 1188, 23-46.
    • (2014) Methods Mol. Biol. , vol.1188 , pp. 23-46
    • Oeljeklaus, S.1    Schummer, A.2    Suppanz, I.3    Warscheid, B.4
  • 147
    • 33751230224 scopus 로고    scopus 로고
    • Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK)
    • Selbach, M., Mann, M., Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK). Nat. Methods 2006, 3, 981-983.
    • (2006) Nat. Methods , vol.3 , pp. 981-983
    • Selbach, M.1    Mann, M.2
  • 148
    • 78149396586 scopus 로고    scopus 로고
    • Identification of novel 14-3-3zeta interacting proteins by quantitative immunoprecipitation combined with knockdown (QUICK)
    • Ge, F., Li, W. L., Bi, L. J., Tao, S. C. et al., Identification of novel 14-3-3zeta interacting proteins by quantitative immunoprecipitation combined with knockdown (QUICK). J. Proteome Res. 2010, 9, 5848-5858.
    • (2010) J. Proteome Res. , vol.9 , pp. 5848-5858
    • Ge, F.1    Li, W.L.2    Bi, L.J.3    Tao, S.C.4
  • 149
    • 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. et al., QUICK identification and SPR validation of signal transducers and activators of transcription 3 (Stat3) interacting proteins. J. Proteomics 2012, 75, 1055-1066.
    • (2012) J. Proteomics , vol.75 , pp. 1055-1066
    • Zheng, P.1    Zhong, Q.2    Xiong, Q.3    Yang, M.4
  • 150
    • 84885154570 scopus 로고    scopus 로고
    • Bcl2-associated athanogene 3 interactome analysis reveals a new role in modulating proteasome activity
    • Chen, Y., Yang, L. N., Cheng, L., Tu, S. et al., Bcl2-associated athanogene 3 interactome analysis reveals a new role in modulating proteasome activity. Mol. Cell. Proteomics 2013, 12, 2804-2819.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 2804-2819
    • Chen, Y.1    Yang, L.N.2    Cheng, L.3    Tu, S.4
  • 151
    • 52649157711 scopus 로고    scopus 로고
    • Combined use of RNAi and quantitative proteomics to study gene function in Drosophila
    • Bonaldi, T., Straub, T., Cox, J., Kumar, C. et al., Combined use of RNAi and quantitative proteomics to study gene function in Drosophila. Mol. Cell 2008, 31, 762-772.
    • (2008) Mol. Cell , vol.31 , pp. 762-772
    • Bonaldi, T.1    Straub, T.2    Cox, J.3    Kumar, C.4
  • 152
    • 84856635802 scopus 로고    scopus 로고
    • Triple SILAC to determine stimulus specific interactions in the Wnt pathway
    • Hilger, M., Mann, M., Triple SILAC to determine stimulus specific interactions in the Wnt pathway. J. Proteome Res. 2011, 11, 982-994.
    • (2011) J. Proteome Res. , vol.11 , pp. 982-994
    • Hilger, M.1    Mann, M.2
  • 153
    • 84925884234 scopus 로고    scopus 로고
    • Defining dynamic protein interactions using SILAC-based quantitative mass spectrometry
    • Wang, X., Huang, L., Defining dynamic protein interactions using SILAC-based quantitative mass spectrometry. Methods Mol. Biol. 2014, 1188, 191-205.
    • (2014) Methods Mol. Biol. , vol.1188 , pp. 191-205
    • Wang, X.1    Huang, L.2
  • 154
    • 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., Discrimination between stable and dynamic components of protein complexes by means of quantitative proteomics. Proteomics 2008, 8, 2366-2370.
    • (2008) Proteomics , vol.8 , pp. 2366-2370
    • Kito, K.1    Kawaguchi, N.2    Okada, S.3    Ito, T.4
  • 155
    • 39049117451 scopus 로고    scopus 로고
    • Identifying dynamic interactors of protein complexes by quantitative mass spectrometry
    • Wang, X., Huang, L., Identifying dynamic interactors of protein complexes by quantitative mass spectrometry. Mol. Cell. Proteomics 2008, 7, 46-57.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 46-57
    • Wang, X.1    Huang, L.2
  • 156
    • 58149391409 scopus 로고    scopus 로고
    • Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry
    • Fang, L., Wang, X., Yamoah, K., Chen, P. L. et al., Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry. J. Proteome Res. 2008, 7, 4914-4925.
    • (2008) J. Proteome Res. , vol.7 , pp. 4914-4925
    • Fang, L.1    Wang, X.2    Yamoah, K.3    Chen, P.L.4
  • 157
    • 43849110454 scopus 로고    scopus 로고
    • Quantitative proteomics reveals regulation of dynamic components within TATA-binding protein (TBP) transcription complexes
    • Mousson, F., Kolkman, A., Pijnappel, W. W., Timmers, H. T., Heck, A. J., Quantitative proteomics reveals regulation of dynamic components within TATA-binding protein (TBP) transcription complexes. Mol. Cell. Proteomics 2008, 7, 845-852.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 845-852
    • Mousson, F.1    Kolkman, A.2    Pijnappel, W.W.3    Timmers, H.T.4    Heck, A.J.5
  • 159
    • 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., The phosphotyrosine interactome of the insulin receptor family and its substrates IRS-1 and IRS-2. Mol. Cell. Proteomics 2009, 8, 519-534.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 519-534
    • Hanke, S.1    Mann, M.2
  • 160
    • 59949099230 scopus 로고    scopus 로고
    • A SILAC-based DNA protein interaction screen that identifies candidate binding proteins to functional DNA elements
    • Mittler, G., Butter, F., Mann, M., A SILAC-based DNA protein interaction screen that identifies candidate binding proteins to functional DNA elements. Genome Res. 2009, 19, 284-293.
    • (2009) Genome Res. , vol.19 , pp. 284-293
    • Mittler, G.1    Butter, F.2    Mann, M.3
  • 161
    • 84887021003 scopus 로고    scopus 로고
    • A DNA-centric protein interaction map of ultraconserved elements reveals contribution of transcription factor binding hubs to conservation
    • Viturawong, T., Meissner, F., Butter, F., Mann, M., A DNA-centric protein interaction map of ultraconserved elements reveals contribution of transcription factor binding hubs to conservation. Cell Rep. 2013, 5, 531-545.
    • (2013) Cell Rep. , vol.5 , pp. 531-545
    • Viturawong, T.1    Meissner, F.2    Butter, F.3    Mann, M.4
  • 162
    • 67649774581 scopus 로고    scopus 로고
    • Unbiased RNA-protein interaction screen by quantitative proteomics
    • Butter, F., Scheibe, M., Morl, M., Mann, M., Unbiased RNA-protein interaction screen by quantitative proteomics. Proc. Natl. Acad. Sci. USA 2009, 106, 10626-10631.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 10626-10631
    • Butter, F.1    Scheibe, M.2    Morl, M.3    Mann, M.4
  • 163
    • 79953321612 scopus 로고    scopus 로고
    • Quantitative profiling of in vivo-assembled RNA-protein complexes using a novel integrated proteomic approach
    • M110007385
    • Tsai, B. P., Wang, X., Huang, L., Waterman, M. L., Quantitative profiling of in vivo-assembled RNA-protein complexes using a novel integrated proteomic approach. Mol. Cell. Proteomics 2011, 10, M110.007385.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Tsai, B.P.1    Wang, X.2    Huang, L.3    Waterman, M.L.4
  • 164
    • 63849172494 scopus 로고    scopus 로고
    • Identifying the proteins to which small-molecule probes and drugs bind in cells
    • Ong, S. E., Schenone, M., Margolin, A. A., Li, X. et al., Identifying the proteins to which small-molecule probes and drugs bind in cells. Proc. Natl. Acad. Sci. USA 2009, 106, 4617-4622.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4617-4622
    • Ong, S.E.1    Schenone, M.2    Margolin, A.A.3    Li, X.4
  • 165
    • 82355165009 scopus 로고    scopus 로고
    • Identifying cellular targets of small-molecule probes and drugs with biochemical enrichment and SILAC
    • Ong, S. E., Li, X., Schenone, M., Schreiber, S. L., Carr, S. A., Identifying cellular targets of small-molecule probes and drugs with biochemical enrichment and SILAC. Methods Mol. Biol. 2012, 803, 129-140.
    • (2012) Methods Mol. Biol. , vol.803 , pp. 129-140
    • Ong, S.E.1    Li, X.2    Schenone, M.3    Schreiber, S.L.4    Carr, S.A.5
  • 167
    • 0015389777 scopus 로고
    • An appraisal of techniques for the determination of protein turnover in vivo
    • Garlick, P. J., Millward, D. J., An appraisal of techniques for the determination of protein turnover in vivo. Biochem. J. 1972, 129, 1P.
    • (1972) Biochem. J. , vol.129 , pp. 1P
    • Garlick, P.J.1    Millward, D.J.2
  • 168
    • 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., The turnover kinetics of major histocompatibility complex peptides of human cancer cells. Mol. Cell. Proteomics 2006, 5, 357-365.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 357-365
    • Milner, E.1    Barnea, E.2    Beer, I.3    Admon, A.4
  • 169
    • 34247391127 scopus 로고    scopus 로고
    • Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins
    • Lam, Y. W., Lamond, A. I., Mann, M., Andersen, J. S., Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins. Curr. Biol. 2007, 17, 749-760.
    • (2007) Curr. Biol. , vol.17 , pp. 749-760
    • Lam, Y.W.1    Lamond, A.I.2    Mann, M.3    Andersen, J.S.4
  • 170
    • 59449085150 scopus 로고    scopus 로고
    • Global analysis of cellular protein translation by pulsed SILAC
    • Schwanhausser, B., Gossen, M., Dittmar, G., Selbach, M., Global analysis of cellular protein translation by pulsed SILAC. Proteomics 2009, 9, 205-209.
    • (2009) Proteomics , vol.9 , pp. 205-209
    • Schwanhausser, B.1    Gossen, M.2    Dittmar, G.3    Selbach, M.4
  • 171
    • 60849097304 scopus 로고    scopus 로고
    • Turnover of the human proteome: determination of protein intracellular stability by dynamic SILAC
    • Doherty, M. K., Hammond, D. E., Clague, M. J., Gaskell, S. J., Beynon, R. J., Turnover of the human proteome: determination of protein intracellular stability by dynamic SILAC. J. Proteome Res. 2009, 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
  • 172
    • 84857963102 scopus 로고    scopus 로고
    • A quantitative spatial proteomics analysis of proteome turnover in human cells
    • M111011429
    • Boisvert, F. M., Ahmad, Y., Gierlinski, M., Charriere, F. et al., A quantitative spatial proteomics analysis of proteome turnover in human cells. Mol. Cell. Proteomics 2011, 11, M111.011429.
    • (2011) Mol. Cell. Proteomics , vol.11
    • Boisvert, F.M.1    Ahmad, Y.2    Gierlinski, M.3    Charriere, F.4
  • 173
    • 84859601514 scopus 로고    scopus 로고
    • C-terminal heat shock protein 90 inhibitor decreases hyperglycemia-induced oxidative stress and improves mitochondrial bioenergetics in sensory neurons
    • Zhang, L., Zhao, H., Blagg, B. S., Dobrowsky, R. T., C-terminal heat shock protein 90 inhibitor decreases hyperglycemia-induced oxidative stress and improves mitochondrial bioenergetics in sensory neurons. J. Proteome Res. 2012, 11, 2581-2593.
    • (2012) J. Proteome Res. , vol.11 , pp. 2581-2593
    • Zhang, L.1    Zhao, H.2    Blagg, B.S.3    Dobrowsky, R.T.4
  • 174
    • 78649698079 scopus 로고    scopus 로고
    • Global turnover of histone post-translational modifications and variants in human cells
    • Zee, B. M., Levin, R. S., Dimaggio, P. A., Garcia, B. A., Global turnover of histone post-translational modifications and variants in human cells. Epigenetics Chromatin. 2010, 3, 22.
    • (2010) Epigenetics Chromatin. , vol.3 , pp. 22
    • Zee, B.M.1    Levin, R.S.2    Dimaggio, P.A.3    Garcia, B.A.4
  • 175
    • 84860805752 scopus 로고    scopus 로고
    • Stable isotope-labelling analysis of the impact of inhibition of the mammalian target of rapamycin on protein synthesis
    • Huo, Y., Iadevaia, V., Yao, Z., Kelly, I. et al., Stable isotope-labelling analysis of the impact of inhibition of the mammalian target of rapamycin on protein synthesis. Biochem. J. 2012, 444, 141-151.
    • (2012) Biochem. J. , vol.444 , pp. 141-151
    • Huo, Y.1    Iadevaia, V.2    Yao, Z.3    Kelly, I.4
  • 176
    • 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, L. P., Chen, L., Nielsen, M. O., Qanie, D. W. et al., Temporal profiling and pulsed SILAC labeling identify novel secreted proteins during ex vivo osteoblast differentiation of human stromal stem cells. Mol. Cell. Proteomics 2012, 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
  • 177
    • 84895546189 scopus 로고    scopus 로고
    • Rapid temporal dynamics of transcription, protein synthesis, and secretion during macrophage activation
    • Eichelbaum, K., Krijgsveld, J., Rapid temporal dynamics of transcription, protein synthesis, and secretion during macrophage activation. Mol. Cell. Proteomics 2014, 13, 792-810.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 792-810
    • Eichelbaum, K.1    Krijgsveld, J.2
  • 178
    • 49949117302 scopus 로고    scopus 로고
    • Widespread changes in protein synthesis induced by microRNAs
    • Selbach, M., Schwanhausser, B., Thierfelder, N., Fang, Z. et al., Widespread changes in protein synthesis induced by microRNAs. Nature 2008, 455, 58-63.
    • (2008) Nature , vol.455 , pp. 58-63
    • Selbach, M.1    Schwanhausser, B.2    Thierfelder, N.3    Fang, Z.4
  • 179
    • 49949116902 scopus 로고    scopus 로고
    • The impact of microRNAs on protein output
    • Baek, D., Villen, J., Shin, C., Camargo, F. D. et al., The impact of microRNAs on protein output. Nature 2008, 455, 64-71.
    • (2008) Nature , vol.455 , pp. 64-71
    • Baek, D.1    Villen, J.2    Shin, C.3    Camargo, F.D.4
  • 180
    • 80051569933 scopus 로고    scopus 로고
    • Whole cell proteome regulation by microRNAs captured in a pulsed SILAC mass spectrometry approach
    • Ebner, O. A., Selbach, M., Whole cell proteome regulation by microRNAs captured in a pulsed SILAC mass spectrometry approach. Methods Mol. Biol. 2011, 725, 315-331.
    • (2011) Methods Mol. Biol. , vol.725 , pp. 315-331
    • Ebner, O.A.1    Selbach, M.2
  • 181
    • 80051613002 scopus 로고    scopus 로고
    • Genome-wide characterization of miR-34a induced changes in protein and mRNA expression by a combined pulsed SILAC and microarray analysis
    • M111010462
    • Kaller, M., Liffers, S. T., Oeljeklaus, S., Kuhlmann, K. et al., Genome-wide characterization of miR-34a induced changes in protein and mRNA expression by a combined pulsed SILAC and microarray analysis. Mol. Cell. Proteomics 2011, 10, M111.010462.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Kaller, M.1    Liffers, S.T.2    Oeljeklaus, S.3    Kuhlmann, K.4
  • 182
    • 84864137161 scopus 로고    scopus 로고
    • In vivo quantitative proteome profiling: planning and evaluation of SILAC experiments
    • Kirchner, M., Selbach, M., In vivo quantitative proteome profiling: planning and evaluation of SILAC experiments. Methods Mol. Biol. 2012, 893, 175-199.
    • (2012) Methods Mol. Biol. , vol.893 , pp. 175-199
    • Kirchner, M.1    Selbach, M.2
  • 184
    • 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. 2002, 37, 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
  • 185
    • 44649164495 scopus 로고    scopus 로고
    • Monitoring of changes in the membrane proteome during stationary phase adaptation of Bacillus subtilis using in vivo labeling techniques
    • Dreisbach, A., Otto, A., Becher, D., Hammer, E. et al., Monitoring of changes in the membrane proteome during stationary phase adaptation of Bacillus subtilis using in vivo labeling techniques. Proteomics 2008, 8, 2062-2076.
    • (2008) Proteomics , vol.8 , pp. 2062-2076
    • Dreisbach, A.1    Otto, A.2    Becher, D.3    Hammer, E.4
  • 186
    • 77954371891 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis
    • Soufi, B., Kumar, C., Gnad, F., Mann, M. et al., Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis. J. Proteome Res. 2010, 9, 3638-3646.
    • (2010) J. Proteome Res. , vol.9 , pp. 3638-3646
    • Soufi, B.1    Kumar, C.2    Gnad, F.3    Mann, M.4
  • 187
    • 0036665484 scopus 로고    scopus 로고
    • Quantitative analysis of the yeast proteome by incorporation of isotopically labeled leucine
    • Jiang, H., English, A. M., Quantitative analysis of the yeast proteome by incorporation of isotopically labeled leucine. J. Proteome Res. 2002, 1, 345-350.
    • (2002) J. Proteome Res. , vol.1 , pp. 345-350
    • Jiang, H.1    English, A.M.2
  • 188
    • 55249096894 scopus 로고    scopus 로고
    • Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast
    • de Godoy, L. M., Olsen, J. V., Cox, J., Nielsen, M. L. et al., Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast. Nature 2008, 455, 1251-1254.
    • (2008) Nature , vol.455 , pp. 1251-1254
    • de Godoy, L.M.1    Olsen, J.V.2    Cox, J.3    Nielsen, M.L.4
  • 189
    • 84871874013 scopus 로고    scopus 로고
    • Comparative proteomics of two life cycle stages of stable isotope-labeled Trypanosoma brucei reveals novel components of the parasite's host adaptation machinery
    • Butter, F., Bucerius, F., Michel, M., Cicova, Z. et al., Comparative proteomics of two life cycle stages of stable isotope-labeled Trypanosoma brucei reveals novel components of the parasite's host adaptation machinery. Mol. Cell. Proteomics 2013, 12, 172-179.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 172-179
    • Butter, F.1    Bucerius, F.2    Michel, M.3    Cicova, Z.4
  • 190
    • 28644448658 scopus 로고    scopus 로고
    • Stable isotope labeling of Arabidopsis thaliana cells and quantitative proteomics by mass spectrometry
    • Gruhler, A., Schulze, W. X., Matthiesen, R., Mann, M., Jensen, O. N., Stable isotope labeling of Arabidopsis thaliana cells and quantitative proteomics by mass spectrometry. Mol. Cell. Proteomics 2005, 4, 1697-1709.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1697-1709
    • Gruhler, A.1    Schulze, W.X.2    Matthiesen, R.3    Mann, M.4    Jensen, O.N.5
  • 191
    • 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 2010, 9, 2173-2183.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2173-2183
    • Sury, M.D.1    Chen, J.X.2    Selbach, M.3
  • 192
    • 84877155520 scopus 로고    scopus 로고
    • Evaluation of Drosophila metabolic labeling strategies for in vivo quantitative proteomic analyses with applications to early pupa formation and amino acid starvation
    • Chang, Y. C., Tang, H. W., Liang, S. Y., Pu, T. H. et al., Evaluation of Drosophila metabolic labeling strategies for in vivo quantitative proteomic analyses with applications to early pupa formation and amino acid starvation. J. Proteome Res. 2013, 12, 2138-2150.
    • (2013) J. Proteome Res. , vol.12 , pp. 2138-2150
    • Chang, Y.C.1    Tang, H.W.2    Liang, S.Y.3    Pu, T.H.4
  • 193
    • 80053369492 scopus 로고    scopus 로고
    • Quantitative proteomics by amino acid labeling in C. elegans
    • Fredens, J., Engholm-Keller, K., Giessing, A., Pultz, D. et al., Quantitative proteomics by amino acid labeling in C. elegans. Nat. Methods 2011, 8, 845-847.
    • (2011) Nat. Methods , vol.8 , pp. 845-847
    • Fredens, J.1    Engholm-Keller, K.2    Giessing, A.3    Pultz, D.4
  • 194
    • 80053363595 scopus 로고    scopus 로고
    • Stable-isotope labeling with amino acids in nematodes
    • Larance, M., Bailly, A. P., Pourkarimi, E., Hay, R. T. et al., Stable-isotope labeling with amino acids in nematodes. Nat. Methods 2011, 8, 849-851.
    • (2011) Nat. Methods , vol.8 , pp. 849-851
    • Larance, M.1    Bailly, A.P.2    Pourkarimi, E.3    Hay, R.T.4
  • 195
    • 82355185718 scopus 로고    scopus 로고
    • SILAC zebrafish for quantitative analysis of protein turnover and tissue regeneration
    • Westman-Brinkmalm, A., Abramsson, A., Pannee, J., Gang, C. et al., SILAC zebrafish for quantitative analysis of protein turnover and tissue regeneration. J. Proteomics 2011, 75, 425-434.
    • (2011) J. Proteomics , vol.75 , pp. 425-434
    • Westman-Brinkmalm, A.1    Abramsson, A.2    Pannee, J.3    Gang, C.4
  • 196
    • 84878722381 scopus 로고    scopus 로고
    • Stable isotope labeling in zebrafish allows in vivo monitoring of cardiac morphogenesis
    • Konzer, A., Ruhs, A., Braun, H., Jungblut, B. et al., Stable isotope labeling in zebrafish allows in vivo monitoring of cardiac morphogenesis. Mol. Cell. Proteomics 2013, 12, 1502-1512.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 1502-1512
    • Konzer, A.1    Ruhs, A.2    Braun, H.3    Jungblut, B.4
  • 197
    • 47549099572 scopus 로고    scopus 로고
    • SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function
    • Kruger, M., Moser, M., Ussar, S., Thievessen, I. et al., SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function. Cell 2008, 134, 353-364.
    • (2008) Cell , vol.134 , pp. 353-364
    • Kruger, M.1    Moser, M.2    Ussar, S.3    Thievessen, I.4
  • 198
    • 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 2010, 9, 11-24.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 11-24
    • Gouw, J.W.1    Krijgsveld, J.2    Heck, A.J.3
  • 199
    • 84877590257 scopus 로고    scopus 로고
    • Identification of disease specific pathways using in vivo SILAC proteomics in dystrophin deficient mdx mouse
    • Rayavarapu, S., Coley, W., Cakir, E., Jahnke, V. et al., Identification of disease specific pathways using in vivo SILAC proteomics in dystrophin deficient mdx mouse. Mol. Cell. Proteomics 2013, 12, 1061-1073.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 1061-1073
    • Rayavarapu, S.1    Coley, W.2    Cakir, E.3    Jahnke, V.4
  • 200
    • 84859562759 scopus 로고    scopus 로고
    • Regulation of lipid metabolism by Dicer revealed through SILAC mice
    • Huang, T. C., Sahasrabuddhe, N. A., Kim, M. S., Getnet, D. et al., Regulation of lipid metabolism by Dicer revealed through SILAC mice. J. Proteome Res. 2012, 11, 2193-2205.
    • (2012) J. Proteome Res. , vol.11 , pp. 2193-2205
    • Huang, T.C.1    Sahasrabuddhe, N.A.2    Kim, M.S.3    Getnet, D.4
  • 201
    • 84886906404 scopus 로고    scopus 로고
    • Global protein quantification of mouse heart tissue based on the SILAC mouse
    • Konzer, A., Ruhs, A., Braun, T., Kruger, M., Global protein quantification of mouse heart tissue based on the SILAC mouse. Methods Mol. Biol. 2013, 1005, 39-52.
    • (2013) Methods Mol. Biol. , vol.1005 , pp. 39-52
    • Konzer, A.1    Ruhs, A.2    Braun, T.3    Kruger, M.4
  • 202
    • 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. et al., Quantitative mouse brain proteomics using culture-derived isotope tags as internal standards. Nat. Biotechnol. 2005, 23, 617-621.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 617-621
    • Ishihama, Y.1    Sato, T.2    Tabata, T.3    Miyamoto, N.4
  • 203
    • 63049110388 scopus 로고    scopus 로고
    • Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type-specific functions
    • Pan, C., Kumar, C., Bohl, S., Klingmueller, U., Mann, M., Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type-specific functions. Mol. Cell. Proteomics 2009, 8, 443-450.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 443-450
    • Pan, C.1    Kumar, C.2    Bohl, S.3    Klingmueller, U.4    Mann, M.5
  • 204
    • 70349490370 scopus 로고    scopus 로고
    • Proteome differences between brown and white fat mitochondria reveal specialized metabolic functions
    • Forner, F., Kumar, C., Luber, C. A., Fromme, T. et al., Proteome differences between brown and white fat mitochondria reveal specialized metabolic functions. Cell Metab. 2009, 10, 324-335.
    • (2009) Cell Metab. , vol.10 , pp. 324-335
    • Forner, F.1    Kumar, C.2    Luber, C.A.3    Fromme, T.4
  • 205
    • 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., Large-scale phosphosite quantification in tissues by a spike-in SILAC method. Nat. Methods 2011, 8, 655-658.
    • (2011) Nat. Methods , vol.8 , pp. 655-658
    • Monetti, M.1    Nagaraj, N.2    Sharma, K.3    Mann, M.4
  • 206
    • 84921467018 scopus 로고    scopus 로고
    • Super-SILAC: current trends and future perspectives
    • Shenoy, A., Geiger, T., Super-SILAC: current trends and future perspectives. Expert Rev. Proteomics 2015, 12, 13-19.
    • (2015) Expert Rev. Proteomics , vol.12 , pp. 13-19
    • Shenoy, A.1    Geiger, T.2
  • 207
    • 84878741907 scopus 로고    scopus 로고
    • Initial quantitative proteomic map of 28 mouse tissues using the SILAC mouse
    • Geiger, T., Velic, A., Macek, B., Lundberg, E. et al., Initial quantitative proteomic map of 28 mouse tissues using the SILAC mouse. Mol. Cell. Proteomics 2013, 12, 1709-1722.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 1709-1722
    • Geiger, T.1    Velic, A.2    Macek, B.3    Lundberg, E.4
  • 208
    • 84899813575 scopus 로고    scopus 로고
    • Quantitative proteomics of synaptic and nonsynaptic mitochondria: insights for synaptic mitochondrial vulnerability
    • Stauch, K. L., Purnell, P. R., Fox, H. S., Quantitative proteomics of synaptic and nonsynaptic mitochondria: insights for synaptic mitochondrial vulnerability. J. Proteome Res. 2014, 13, 2620-2636.
    • (2014) J. Proteome Res. , vol.13 , pp. 2620-2636
    • Stauch, K.L.1    Purnell, P.R.2    Fox, H.S.3
  • 209
    • 84883001984 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic profiling of human non-small cell lung cancer tumors
    • Schweppe, D. K., Rigas, J. R., Gerber, S. A., Quantitative phosphoproteomic profiling of human non-small cell lung cancer tumors. J. Proteomics 2013, 91, 286-296.
    • (2013) J. Proteomics , vol.91 , pp. 286-296
    • Schweppe, D.K.1    Rigas, J.R.2    Gerber, S.A.3
  • 210
    • 84891773596 scopus 로고    scopus 로고
    • N-linked glycosylation enrichment for in-depth cell surface proteomics of diffuse large B-cell lymphoma subtypes
    • Deeb, S. J., Cox, J., Schmidt-Supprian, M., Mann, M., N-linked glycosylation enrichment for in-depth cell surface proteomics of diffuse large B-cell lymphoma subtypes. Mol. Cell. Proteomics 2014, 13, 240-251.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 240-251
    • Deeb, S.J.1    Cox, J.2    Schmidt-Supprian, M.3    Mann, M.4
  • 211
    • 84861157792 scopus 로고    scopus 로고
    • Super-SILAC allows classification of diffuse large B-cell lymphoma subtypes by their protein expression profiles
    • Deeb, S. J., D'Souza, R. C., Cox, J., Schmidt-Supprian, M., Mann, M., Super-SILAC allows classification of diffuse large B-cell lymphoma subtypes by their protein expression profiles. Mol. Cell. Proteomics 2012, 11, 77-89.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 77-89
    • Deeb, S.J.1    D'Souza, R.C.2    Cox, J.3    Schmidt-Supprian, M.4    Mann, M.5
  • 212
    • 84895760967 scopus 로고    scopus 로고
    • Proteomic profiles of human lung adeno and squamous cell carcinoma using super-SILAC and label-free quantification approaches
    • Zhang, W., Wei, Y., Ignatchenko, V., Li, L. et al., Proteomic profiles of human lung adeno and squamous cell carcinoma using super-SILAC and label-free quantification approaches. Proteomics 2014, 14, 795-803.
    • (2014) Proteomics , vol.14 , pp. 795-803
    • Zhang, W.1    Wei, Y.2    Ignatchenko, V.3    Li, L.4
  • 213
    • 84864017230 scopus 로고    scopus 로고
    • Quantitative proteomics of primary tumors with varying metastatic capabilities using stable isotope-labeled proteins of multiple histogenic origins
    • Lund, R. R., Terp, M. G., Laenkholm, A. V., Jensen, O. N. et al., Quantitative proteomics of primary tumors with varying metastatic capabilities using stable isotope-labeled proteins of multiple histogenic origins. Proteomics 2012, 12, 2139-2148.
    • (2012) Proteomics , vol.12 , pp. 2139-2148
    • Lund, R.R.1    Terp, M.G.2    Laenkholm, A.V.3    Jensen, O.N.4
  • 215
    • 84875716859 scopus 로고    scopus 로고
    • Neutron-encoded mass signatures for multiplexed proteome quantification
    • Hebert, A. S., Merrill, A. E., Bailey, D. J., Still, A. J. et al., Neutron-encoded mass signatures for multiplexed proteome quantification. Nat. Methods 2013, 10, 332-334.
    • (2013) Nat. Methods , vol.10 , pp. 332-334
    • Hebert, A.S.1    Merrill, A.E.2    Bailey, D.J.3    Still, A.J.4
  • 217
    • 84910682140 scopus 로고    scopus 로고
    • Broader implications of SILAC-based proteomics for dissecting signaling dynamics in cancer
    • Zhang, H., Xu, Y., Papanastasopoulos, P., Stebbing, J., Giamas, G., Broader implications of SILAC-based proteomics for dissecting signaling dynamics in cancer. Expert Rev. Proteomics 2014, 11, 713-731.
    • (2014) Expert Rev. Proteomics , vol.11 , pp. 713-731
    • Zhang, H.1    Xu, Y.2    Papanastasopoulos, P.3    Stebbing, J.4    Giamas, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.