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Volumn 12, Issue 5, 2013, Pages 1115-1126

Protein correlation profiles identify lipid droplet proteins with high confidence

Author keywords

[No Author keywords available]

Indexed keywords

FAT DROPLET; PROTEOME;

EID: 84875367136     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.020230     Document Type: Article
Times cited : (131)

References (56)
  • 1
    • 84861897793 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics and network biology
    • Bensimon, A., Heck, A. J., and Aebersold, R. (2012) Mass spectrometry-based proteomics and network biology. Annu. Rev. Biochem. 81, 379-405
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 379-405
    • Bensimon, A.1    Heck, A.J.2    Aebersold, R.3
  • 2
    • 60649097712 scopus 로고    scopus 로고
    • Evolution of organelle-associated protein profiling
    • Yan, W., Aebersold, R., and Raines, E. W. (2009) Evolution of organelle-associated protein profiling. J. Proteomics 72, 4-11
    • (2009) J. Proteomics , vol.72 , pp. 4-11
    • Yan, W.1    Aebersold, R.2    Raines, E.W.3
  • 3
    • 77955876447 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics in cell biology
    • Walther, T. C., and Mann, M. (2010) Mass spectrometry-based proteomics in cell biology. J. Cell. Biol. 190, 491-500
    • (2010) J. Cell. Biol. , vol.190 , pp. 491-500
    • Walther, T.C.1    Mann, M.2
  • 4
    • 70449769682 scopus 로고    scopus 로고
    • Lipid droplets finally get a little R-E-S-P-E-C-T
    • Farese, R. V., Jr., and Walther, T. C. (2009) Lipid droplets finally get a little R-E-S-P-E-C-T. Cell 139, 855-860
    • (2009) Cell , vol.139 , pp. 855-860
    • Farese Jr., R.V.1    Walther, T.C.2
  • 5
    • 79960636348 scopus 로고    scopus 로고
    • Not just fat: The structure and function of the lipid droplet
    • Fujimoto, T., and Parton, R. G. (2011) Not just fat: the structure and function of the lipid droplet. Cold Spring Harb. Perspect. Biol. 3, a004838
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3
    • Fujimoto, T.1    Parton, R.G.2
  • 6
    • 84856072854 scopus 로고    scopus 로고
    • Packaging of fat: An evolving model of lipid droplet assembly and expansion
    • Brasaemle, D. L., and Wolins, N. E. (2012) Packaging of fat: an evolving model of lipid droplet assembly and expansion. J. Biol. Chem. 287, 2273-2279
    • (2012) J. Biol. Chem. , vol.287 , pp. 2273-2279
    • Brasaemle, D.L.1    Wolins, N.E.2
  • 7
    • 79958815982 scopus 로고    scopus 로고
    • Unique ties between hepatitis C virus replication and intracellular lipids
    • Herker, E., and Ott, M. (2011) Unique ties between hepatitis C virus replication and intracellular lipids. Trends Endocrinol. Metab. 22, 241-248
    • (2011) Trends Endocrinol. Metab. , vol.22 , pp. 241-248
    • Herker, E.1    Ott, M.2
  • 11
    • 33748598240 scopus 로고    scopus 로고
    • The Lipid-Droplet Proteome Reveals that Droplets Are a Protein-Storage Depot
    • DOI 10.1016/j.cub.2006.07.062, PII S0960982206019750
    • Cermelli, S., Guo, Y., Gross, S. P., and Welte, M. A. (2006) The lipid-droplet proteome reveals that droplets are a protein-storage depot. Curr. Biol. 16, 1783-1795 (Pubitemid 44376718)
    • (2006) Current Biology , vol.16 , Issue.18 , pp. 1783-1795
    • Cermelli, S.1    Guo, Y.2    Gross, S.P.3    Welte, M.A.4
  • 12
    • 80053062569 scopus 로고    scopus 로고
    • Interactomic study on interaction between lipid droplets and mitochondria
    • Pu, J., Ha, C. W., Zhang, S., Jung, J. P., Huh, W. K., and Liu, P. (2011) Interactomic study on interaction between lipid droplets and mitochondria. Protein Cell 2, 487-496
    • (2011) Protein Cell , vol.2 , pp. 487-496
    • Pu, J.1    Ha, C.W.2    Zhang, S.3    Jung, J.P.4    Huh, W.K.5    Liu, P.6
  • 13
    • 8744267532 scopus 로고    scopus 로고
    • Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes
    • DOI 10.1074/jbc.M409340200
    • Brasaemle, D. L., Dolios, G., Shapiro, L., and Wang, R. (2004) Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes. J. Biol. Chem. 279, 46835-46842 (Pubitemid 39518334)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.45 , pp. 46835-46842
    • Brasaemle, D.L.1    Dolios, G.2    Shapiro, L.3    Wang, R.4
  • 14
    • 84860436155 scopus 로고    scopus 로고
    • Proteomic profiling of lipid droplet-associated proteins in primary adipocytes of normal and obese mouse
    • Ding, Y., Wu, Y., Zeng, R., and Liao, K. (2012) Proteomic profiling of lipid droplet-associated proteins in primary adipocytes of normal and obese mouse. Acta Biochim. Biophys. Sin. (Shanghai)
    • (2012) Acta Biochim. Biophys. Sin. (Shanghai)
    • Ding, Y.1    Wu, Y.2    Zeng, R.3    Liao, K.4
  • 15
    • 84856656225 scopus 로고    scopus 로고
    • Characterization of the lipid droplet proteome of a clonal insulin-producing beta-cell line (INS-1 832/13)
    • Larsson, S., Resjo, S., Gomez, M. F., James, P., and Holm, C. (2012) Characterization of the lipid droplet proteome of a clonal insulin-producing beta-cell line (INS-1 832/13). J. Proteome Res. 11, 1264-1273
    • (2012) J. Proteome Res. , vol.11 , pp. 1264-1273
    • Larsson, S.1    Resjo, S.2    Gomez, M.F.3    James, P.4    Holm, C.5
  • 16
    • 80053909233 scopus 로고    scopus 로고
    • Proteome of skeletal muscle lipid droplet reveals association with mitochondria and apolipoprotein a-I
    • Zhang, H., Wang, Y., Li, J., Yu, J., Pu, J., Li, L., Zhang, S., Peng, G., Yang, F., and Liu, P. (2011) Proteome of skeletal muscle lipid droplet reveals association with mitochondria and apolipoprotein a-I. J. Proteome Res. 10, 4757-4768
    • (2011) J. Proteome Res. , vol.10 , pp. 4757-4768
    • Zhang, H.1    Wang, Y.2    Li, J.3    Yu, J.4    Pu, J.5    Li, L.6    Zhang, S.7    Peng, G.8    Yang, F.9    Liu, P.10
  • 18
    • 34548150017 scopus 로고    scopus 로고
    • Dynamic activity of lipid droplets: Protein phosphorylation and GTP-mediated protein translocation
    • DOI 10.1021/pr070158j
    • Bartz, R., Zehmer, J. K., Zhu, M., Chen, Y., Serrero, G., Zhao, Y., and Liu, P. (2007) Dynamic activity of lipid droplets: protein phosphorylation and GTP-mediated protein translocation. J. Proteome Res. 6, 3256-3265 (Pubitemid 47310210)
    • (2007) Journal of Proteome Research , vol.6 , Issue.8 , pp. 3256-3265
    • Bartz, R.1    Zehmer, J.K.2    Zhu, M.3    Chen, Y.4    Serrero, G.5    Zhao, Y.6    Liu, P.7
  • 19
    • 0942287191 scopus 로고    scopus 로고
    • Chinese Hamster Ovary K2 Cell Lipid Droplets Appear to be Metabolic Organelles Involved in Membrane Traffic
    • DOI 10.1074/jbc.M311945200
    • Liu, P., Ying, Y., Zhao, Y., Mundy, D. I., Zhu, M., and Anderson, R. G. (2004) Chinese hamster ovary K2 cell lipid droplets appear to be metabolic organelles involved in membrane traffic. J. Biol. Chem. 279, 3787-3792 (Pubitemid 38140623)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3787-3792
    • Liu, P.1    Ying, Y.2    Zhao, Y.3    Mundy, D.I.4    Zhu, M.5    Anderson, R.G.W.6
  • 20
    • 0033769564 scopus 로고    scopus 로고
    • Proteomics reveal a link between the endoplasmic reticulum and lipid secretory mechanisms in mammary epithelial cells
    • Wu, C. C., Howell, K. E., Neville, M. C., Yates, J. R., III, and McManaman, J. L. (2000) Proteomics reveal a link between the endoplasmic reticulum and lipid secretory mechanisms in mammary epithelial cells. Electrophoresis 21, 3470-3482
    • (2000) Electrophoresis , vol.21 , pp. 3470-3482
    • Wu, C.C.1    Howell, K.E.2    Neville, M.C.3    Yates III, J.R.4    McManaman, J.L.5
  • 22
    • 0020569403 scopus 로고
    • Movement of lipolytic products to mitochondria in brown adipose tissue of young rats: An electron microscope study
    • Blanchette-Mackie, E. J., and Scow, R. O. (1983) Movement of lipolytic products to mitochondria in brown adipose tissue of young rats: an electron microscope study. J. Lipid Res. 24, 229-244
    • (1983) J. Lipid Res. , vol.24 , pp. 229-244
    • Blanchette-Mackie, E.J.1    Scow, R.O.2
  • 23
    • 37249058863 scopus 로고    scopus 로고
    • Network distribution of mitochondria and lipid droplets in human muscle fibres
    • DOI 10.1007/s00418-007-0349-8
    • Shaw, C. S., Jones, D. A., and Wagenmakers, A. J. M. (2008) Network distribution of mitochondria and lipid droplets in human muscle fibres. Histochem. Cell Biol. 129, 65-72 (Pubitemid 350276140)
    • (2008) Histochemistry and Cell Biology , vol.129 , Issue.1 , pp. 65-72
    • Shaw, C.S.1    Jones, D.A.2    Wagenmakers, A.J.M.3
  • 24
    • 79960398841 scopus 로고    scopus 로고
    • Lipid droplets are functionally connected to the endoplasmic reticulum in Saccharomyces cerevisiae
    • Jacquier, N., Choudhary, V., Mari, M., Toulmay, A., Reggiori, F., and Schneiter, R. (2011) Lipid droplets are functionally connected to the endoplasmic reticulum in Saccharomyces cerevisiae. J. Cell Sci. 124, 2424-2437
    • (2011) J. Cell Sci. , vol.124 , pp. 2424-2437
    • Jacquier, N.1    Choudhary, V.2    Mari, M.3    Toulmay, A.4    Reggiori, F.5    Schneiter, R.6
  • 25
    • 21644459401 scopus 로고    scopus 로고
    • Rab18 localizes to lipid droplets and induces their close apposition to the endoplasmic reticulum-derived membrane
    • DOI 10.1242/jcs.02401
    • Ozeki, S., Cheng, J., Tauchi-Sato, K., Hatano, N., Taniguchi, H., and Fujimoto, T. (2005) Rab18 localizes to lipid droplets and induces their close apposition to the endoplasmic reticulum-derived membrane. J. Cell Sci. 118, 2601-2611 (Pubitemid 40932886)
    • (2005) Journal of Cell Science , vol.118 , Issue.12 , pp. 2601-2611
    • Ozeki, S.1    Cheng, J.2    Tauchi-Sato, K.3    Hatano, N.4    Taniguchi, H.5    Fujimoto, T.6
  • 26
    • 29644442801 scopus 로고    scopus 로고
    • Regulated localization of Rab18 to lipid droplets: Effects of lipolytic stimulation and inhibition of lipid droplet catabolism
    • DOI 10.1074/jbc.M506651200
    • Martin, S., Driessen, K., Nixon, S. J., Zerial, M., and Parton, R. G. (2005) Regulated localization of Rab18 to lipid droplets: effects of lipolytic stimulation and inhibition of lipid droplet catabolism. J. Biol. Chem. 280, 42325-42335 (Pubitemid 43023204)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.51 , pp. 42325-42335
    • Martin, S.1    Driessen, K.2    Nixon, S.J.3    Zerial, M.4    Parton, R.G.5
  • 29
    • 33749523582 scopus 로고    scopus 로고
    • Organellar proteomics: Turning inventories into insights
    • DOI 10.1038/sj.embor.7400780, PII 7400780
    • Andersen, J. S., and Mann, M. (2006) Organellar proteomics: turning inventories into insights. EMBO Rep. 7, 874-879 (Pubitemid 44523965)
    • (2006) EMBO Reports , vol.7 , Issue.9 , pp. 874-879
    • Andersen, J.S.1    Mann, M.2
  • 32
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • DOI 10.1038/nature02166
    • Andersen, J. S., Wilkinson, C. J., Mayor, T., Mortensen, P., Nigg, E. A., and Mann, M. (2003) Proteomic characterization of the human centrosome by protein correlation profiling. Nature 426, 570-574 (Pubitemid 37522644)
    • (2003) Nature , vol.426 , Issue.6966 , pp. 570-574
    • Andersen, J.S.1    Wilkinson, C.J.2    Mayor, T.3    Mortensen, P.4    Nigg, E.A.5    Mann, M.6
  • 33
    • 33646473345 scopus 로고    scopus 로고
    • A mammalian organelle map by protein correlation profiling
    • Foster, L. J., de Hoog, C. L., Zhang, Y., Xie, X., Mootha, V. K., and Mann, M. (2006) A mammalian organelle map by protein correlation profiling. Cell 125, 187-199
    • (2006) Cell , vol.125 , pp. 187-199
    • Foster, L.J.1    De Hoog, C.L.2    Zhang, Y.3    Xie, X.4    Mootha, V.K.5    Mann, M.6
  • 34
    • 44449095056 scopus 로고    scopus 로고
    • Functional genomic screen reveals genes involved in lipid-droplet formation and utilization
    • DOI 10.1038/nature06928, PII NATURE06928
    • Guo, Y., Walther, T. C., Rao, M., Stuurman, N., Goshima, G., Terayama, K., Wong, J. S., Vale, R. D., Walter, P., and Farese, R. V. (2008) Functional genomic screen reveals genes involved in lipid-droplet formation and utilization. Nature 453, 657-661 (Pubitemid 351769298)
    • (2008) Nature , vol.453 , Issue.7195 , pp. 657-661
    • Guo, Y.1    Walther, T.C.2    Rao, M.3    Stuurman, N.4    Goshima, G.5    Terayama, K.6    Wong, J.S.7    Vale, R.D.8    Walter, P.9    Farese Jr., R.V.10
  • 35
    • 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., Becker, P. B., and Mann, M. (2008) Combined use of RNAi and quantitative proteomics to study gene function in Drosophila. Mol. Cell 31, 762-772
    • (2008) Mol. Cell , vol.31 , pp. 762-772
    • Bonaldi, T.1    Straub, T.2    Cox, J.3    Kumar, C.4    Becker, P.B.5    Mann, M.6
  • 36
    • 39749145871 scopus 로고    scopus 로고
    • Isolation of lipid droplets from cells by density gradient centrifugation
    • Unit 3 15
    • Brasaemle, D. L., and Wolins, N. E. (2006) Isolation of lipid droplets from cells by density gradient centrifugation. Curr. Protoc. Cell. Biol. Chapter 3, Unit 3 15
    • (2006) Curr. Protoc. Cell. Biol. , vol.CHAPTER 3
    • Brasaemle, D.L.1    Wolins, N.E.2
  • 37
    • 0037317228 scopus 로고    scopus 로고
    • Stop And Go Extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • DOI 10.1021/ac026117i
    • Rappsilber, J., Ishihama, Y., and Mann, M. (2003) Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal. Chem. 75, 663-670 (Pubitemid 36176744)
    • (2003) Analytical Chemistry , vol.75 , Issue.3 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 38
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • DOI 10.1038/nprot.2007.261, PII NPROT.2007.261
    • Rappsilber, J., Mann, M., and Ishihama, Y. (2007) Protocol for micropurification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2, 1896-1906 (Pubitemid 47308128)
    • (2007) Nature Protocols , vol.2 , Issue.8 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 39
    • 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., and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 41
    • 22544432531 scopus 로고    scopus 로고
    • Noise-robust soft clustering of gene expression time-course data
    • DOI 10.1142/S0219720005001375, PII S0219720005001375
    • Futschik, M. E., and Carlisle, B. (2005) Noise-robust soft clustering of gene expression time-course data. J. Bioinform. Comput. Biol. 3, 965-988 (Pubitemid 41015297)
    • (2005) Journal of Bioinformatics and Computational Biology , vol.3 , Issue.4 , pp. 965-988
    • Futschik, M.E.1    Carlisle, B.2
  • 42
    • 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., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 44
    • 78649701176 scopus 로고    scopus 로고
    • A buoyancy-based screen of Drosophila larvae for fat-storage mutants reveals a role for Sir2 in coupling fat storage to nutrient availability
    • Reis, T., Van Gilst, M. R., and Hariharan, I. K. (2010) A buoyancy-based screen of Drosophila larvae for fat-storage mutants reveals a role for Sir2 in coupling fat storage to nutrient availability. PLoS Genet. 6, e1001206
    • (2010) PLoS Genet. , vol.6
    • Reis, T.1    Van Gilst, M.R.2    Hariharan, I.K.3
  • 47
    • 34249804498 scopus 로고    scopus 로고
    • Using FlyAtlas to identify better Drosophila melanogaster models of human disease
    • DOI 10.1038/ng2049, PII NG2049
    • Chintapalli, V. R., Wang, J., and Dow, J. A. (2007) Using FlyAtlas to identify better Drosophila melanogaster models of human disease. Nat. Genet. 39, 715-720 (Pubitemid 46848596)
    • (2007) Nature Genetics , vol.39 , Issue.6 , pp. 715-720
    • Chintapalli, V.R.1    Wang, J.2    Dow, J.A.T.3
  • 49
    • 33846279755 scopus 로고    scopus 로고
    • Specialized hepatocyte-like cells regulate Drosophila lipid metabolism
    • DOI 10.1038/nature05382, PII NATURE05382
    • Gutierrez, E., Wiggins, D., Fielding, B., and Gould, A. P. (2007) Specialized hepatocyte-like cells regulate Drosophila lipid metabolism. Nature 445, 275-280 (Pubitemid 46122810)
    • (2007) Nature , vol.445 , Issue.7125 , pp. 275-280
    • Gutierrez, E.1    Wiggins, D.2    Fielding, B.3    Gould, A.P.4
  • 50
    • 0037165138 scopus 로고    scopus 로고
    • Translocation of lipid-linked oligosaccharides across the ER membrane requires Rft1 protein
    • DOI 10.1038/415447a
    • Helenius, J., Ng, D. T., Marolda, C. L., Walter, P., Valvano, M. A., and Aebi, M. (2002) Translocation of lipid-linked oligosaccharides across the ER membrane requires Rft1 protein. Nature 415, 447-450 (Pubitemid 34100957)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 447-450
    • Helenius, J.1    Ng, D.T.W.2    Marolda, C.L.3    Walter, P.4    Valvano, M.A.5    Aebi, M.6
  • 51
    • 80053469048 scopus 로고    scopus 로고
    • Mechanisms and principles of N-linked protein glycosylation
    • Schwarz, F., and Aebi, M. (2011) Mechanisms and principles of N-linked protein glycosylation. Curr. Opin. Struct. Biol. 21, 576-582
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 576-582
    • Schwarz, F.1    Aebi, M.2
  • 52
    • 46349105757 scopus 로고    scopus 로고
    • In vitro formation of a novel type of membrane vesicles containing Dpm1p: Putative transport vesicles for lipid droplets in budding yeast
    • DOI 10.1093/jb/mvn034
    • Takeda, Y., and Nakano, A. (2008) In vitro formation of a novel type of membrane vesicles containing Dpm1p: putative transport vesicles for lipid droplets in budding yeast. J. Biochem. 143, 803-811 (Pubitemid 351918943)
    • (2008) Journal of Biochemistry , vol.143 , Issue.6 , pp. 803-811
    • Takeda, Y.1    Nakano, A.2
  • 53
    • 47549099572 scopus 로고    scopus 로고
    • SILAC Mouse for Quantitative Proteomics Uncovers Kindlin-3 as an Essential Factor for Red Blood Cell Function
    • DOI 10.1016/j.cell.2008.05.033, PII S0092867408006958
    • Kruger, M., Moser, M., Ussar, S., Thievessen, I., Luber, C. A., Forner, F., Schmidt, S., Zanivan, S., Fassler, R., and Mann, M. (2008) SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function. Cell 134, 353-364 (Pubitemid 352010327)
    • (2008) Cell , vol.134 , Issue.2 , pp. 353-364
    • Kruger, M.1    Moser, M.2    Ussar, S.3    Thievessen, I.4    Luber, C.A.5    Forner, F.6    Schmidt, S.7    Zanivan, S.8    Fassler, R.9    Mann, M.10
  • 54
    • 77958018495 scopus 로고    scopus 로고
    • The SILAC fly allows for accurate protein quantification in vivo
    • Sury, M. D., Chen, J. X., and Selbach, M. (2010) The SILAC fly allows for accurate protein quantification in vivo. Mol. Cell. Proteomics 9, 2173-2183
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2173-2183
    • Sury, M.D.1    Chen, J.X.2    Selbach, M.3
  • 55
    • 79961014854 scopus 로고    scopus 로고
    • Large-scale phosphosite quantification in tissues by a spike-in SILAC method
    • Monetti, M., Nagaraj, N., Sharma, K., and Mann, M. (2011) Large-scale phosphosite quantification in tissues by a spike-in SILAC method. Nat. Methods 8, 655-658
    • (2011) Nat. Methods , vol.8 , pp. 655-658
    • Monetti, M.1    Nagaraj, N.2    Sharma, K.3    Mann, M.4
  • 56
    • 77952226764 scopus 로고    scopus 로고
    • Super-SILAC mix for quantitative proteomics of human tumor tissue
    • Geiger, T., Cox, J., Ostasiewicz, P., Wisniewski, J. R., and Mann, M. (2010) Super-SILAC mix for quantitative proteomics of human tumor tissue. Nat. Methods 7, 383-385
    • (2010) Nat. Methods , vol.7 , pp. 383-385
    • Geiger, T.1    Cox, J.2    Ostasiewicz, P.3    Wisniewski, J.R.4    Mann, M.5


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