메뉴 건너뛰기




Volumn 10, Issue 8, 2013, Pages 768-773

Cell-selective labeling using amino acid precursors for proteomic studies of multicellular environments

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ISOTOPE; LYSINE; MESSENGER RNA; PROTEOME;

EID: 84881475017     PISSN: 15487091     EISSN: 15487105     Source Type: Journal    
DOI: 10.1038/nmeth.2529     Document Type: Article
Times cited : (48)

References (35)
  • 1
    • 63049104211 scopus 로고    scopus 로고
    • Microenvironmental regulation of metastasis
    • Joyce, J.A. & Pollard, J.W. Microenvironmental regulation of metastasis. Nat. Rev. Cancer 9, 239-252 (2009).
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 239-252
    • Joyce, J.A.1    Pollard, J.W.2
  • 2
    • 77950542260 scopus 로고    scopus 로고
    • Tumor cell-specifc bioluminescence platform to identify stroma-induced changes to anticancer drug activity
    • Mcmillin, D.W. et al. Tumor cell-specifc bioluminescence platform to identify stroma-induced changes to anticancer drug activity. Nat. Med. 16, 483-489 (2010).
    • (2010) Nat. Med. , vol.16 , pp. 483-489
    • McMillin, D.W.1
  • 5
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S.-E. et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell Proteomics 1, 376-386 (2002).
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.-E.1
  • 6
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross, P.L. et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell Proteomics 3, 1154-1169 (2004).
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1
  • 7
    • 72149101924 scopus 로고    scopus 로고
    • Cell-specifc information processing in segregating populations of Eph receptor ephrin-expressing cells
    • Jørgensen, C. et al. Cell-specifc information processing in segregating populations of Eph receptor ephrin-expressing cells. Science 326, 1502-1509 (2009).
    • (2009) Science , vol.326 , pp. 1502-1509
    • Jørgensen, C.1
  • 8
    • 78049334902 scopus 로고    scopus 로고
    • Trans-SILAC: Sorting out the non-cell-autonomous proteome
    • Rechavi, O. et al. Trans-SILAC: sorting out the non-cell-autonomous proteome. Nat. Methods 7, 923-927 (2010).
    • (2010) Nat. Methods , vol.7 , pp. 923-927
    • Rechavi, O.1
  • 9
    • 84859823928 scopus 로고    scopus 로고
    • The matrisome: In silico defnition and in vivo characterization by proteomics of normal and tumor extracellular matrices
    • Naba, A. et al. The matrisome: in silico defnition and in vivo characterization by proteomics of normal and tumor extracellular matrices. Mol. Cell Proteomics 11, M111.014647 (2012).
    • (2012) Mol. Cell Proteomics , vol.11
    • Naba, A.1
  • 10
    • 33750612210 scopus 로고    scopus 로고
    • Mass spectrometric identifcation of human prostate cancer-derived proteins in serum of xenograft-bearing mice
    • van den Bemd, G.-J.C.M. et al. Mass spectrometric identifcation of human prostate cancer-derived proteins in serum of xenograft-bearing mice. Mol. Cell Proteomics 5, 1830-1839 (2006).
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 1830-1839
    • Van Den Bemd, G.-J.C.M.1
  • 11
    • 70349327398 scopus 로고    scopus 로고
    • Cell-selective metabolic labeling of proteins
    • Ngo, J.T. et al. Cell-selective metabolic labeling of proteins. Nat. Chem. Biol. 5, 715-717 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 715-717
    • Ngo, J.T.1
  • 12
    • 84861361764 scopus 로고    scopus 로고
    • Two-strain, cell-selective protein labeling in mixed bacterial cultures
    • Truong, F., Yoo, T.H., Lampo, T.J. & Tirrell, D.A. Two-strain, cell-selective protein labeling in mixed bacterial cultures. J. Am. Chem. Soc. 134, 8551-8556 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 8551-8556
    • Truong, F.1    Yoo, T.H.2    Lampo, T.J.3    Tirrell, D.A.4
  • 13
    • 84875523875 scopus 로고    scopus 로고
    • Mutant methionyl-tRNA synthetase from bacteria enables site-selective N-terminal labeling of proteins expressed in mammalian cells
    • Ngo, J.T., Schuman, E.M. & Tirrell, D.A. Mutant methionyl-tRNA synthetase from bacteria enables site-selective N-terminal labeling of proteins expressed in mammalian cells. Proc. Natl. Acad. Sci. USA 110, 4992-4997 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 4992-4997
    • Ngo, J.T.1    Schuman, E.M.2    Tirrell, D.A.3
  • 14
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu, C.C. & Schultz, P.G. Adding new chemistries to the genetic code. Annu. Rev. Biochem. 79, 413-444 (2010).
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 15
    • 33748290014 scopus 로고    scopus 로고
    • The α-aminoadipate pathway for lysine biosynthesis in fungi
    • DOI 10.1385/CBB:46:1:43, PII CBB46143
    • Xu, H., Andi, B., Qian, J., West, A.H. & Cook, P.F. The alpha-aminoadipate pathway for lysine biosynthesis in fungi. Cell Biochem. Biophys. 46, 43-64 (2006). (Pubitemid 44326229)
    • (2006) Cell Biochemistry and Biophysics , vol.46 , Issue.1 , pp. 43-64
    • Xu, H.1    Andi, B.2    Qian, J.3    West, A.H.4    Cook, P.F.5
  • 16
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong, S.-E. & Mann, M. A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat. Protoc. 1, 2650-2660 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 2650-2660
    • Ong, S.-E.1    Mann, M.2
  • 18
    • 0021995022 scopus 로고
    • Expression in mammalian cells of the diaminopimelic acid decarboxylase of Escherichia coli permits cell growth in lysine-free medium
    • DOI 10.1111/j.1432-1033.1985.tb08635.x
    • Jouanneau, J., Stragier, P., Bouvier, J., Patte, J.C. & Yaniv, M. Expression in mammalian cells of the diaminopimelic acid decarboxylase of Escherichia coli permits cell growth in lysine-free medium. Eur. J. Biochem. 146, 173-178 (1985). (Pubitemid 15188173)
    • (1985) European Journal of Biochemistry , vol.146 , Issue.1 , pp. 173-178
    • Jouanneau, J.1    Stragier, P.2    Bouvier, J.3
  • 19
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identifcation rates, individualized P.P.B. - Range mass accuracies and proteome-wide protein quantifcation
    • Cox, J. & Mann, M. MaxQuant enables high peptide identifcation rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantifcation. Nat. Biotechnol. 26, 1367-1372 (2008).
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 20
    • 77958018495 scopus 로고    scopus 로고
    • The SILAC fy allows for accurate protein quantifcation in vivo
    • Sury, M.D., Chen, J.-X. & Selbach, M. The SILAC fy allows for accurate protein quantifcation in vivo. Mol. Cell Proteomics 9, 2173-2183 (2010).
    • (2010) Mol. Cell Proteomics , vol.9 , pp. 2173-2183
    • Sury, M.D.1    Chen, J.-X.2    Selbach, M.3
  • 21
    • 45749144385 scopus 로고    scopus 로고
    • Stable isotopic labeling by amino acids in cultured primary neurons: Application to brain-derived neurotrophic factor-dependent phosphotyrosine- associated signaling
    • DOI 10.1074/mcp.M700387-MCP200
    • Spellman, D.S., Deinhardt, K., Darie, C.C., Chao, M.V. & Neubert, T.A. Stable isotopic labeling by amino acids in cultured primary neurons: application to brain-derived neurotrophic factor-dependent phosphotyrosine- associated signaling. Mol. Cell Proteomics 7, 1067-1076 (2008). (Pubitemid 351943954)
    • (2008) Molecular and Cellular Proteomics , vol.7 , Issue.6 , pp. 1067-1076
    • Spellman, D.S.1    Deinhardt, K.2    Darie, C.C.3    Chao, M.V.4    Neuebrt, T.A.5
  • 22
    • 84857938446 scopus 로고    scopus 로고
    • Comparative proteomic analysis of eleven common cell lines reveals ubiquitous but varying expression of most proteins
    • Geiger, T., Wehner, A., Schaab, C., Cox, J. & Mann, M. Comparative proteomic analysis of eleven common cell lines reveals ubiquitous but varying expression of most proteins. Mol Cell Proteomics 11, M111.014050 (2012).
    • (2012) Mol Cell Proteomics , vol.11
    • Geiger, T.1    Wehner, A.2    Schaab, C.3    Cox, J.4    Mann, M.5
  • 23
    • 80052692104 scopus 로고    scopus 로고
    • Biochemical characterization of a novel lysine racemase from Proteus mirabilis BCRC10725
    • Kuan, Y.-C. et al. Biochemical characterization of a novel lysine racemase from Proteus mirabilis BCRC10725. Process Biochem. 46, 1914-1920 (2011).
    • (2011) Process Biochem. , vol.46 , pp. 1914-1920
    • Kuan, Y.-C.1
  • 24
    • 0442292081 scopus 로고    scopus 로고
    • Cloning and expression of a novel enantioselective N-carbobenzyloxy- cleaving enzyme
    • DOI 10.1016/j.enzmictec.2003.11.012
    • Nanduri, V., Goldberg, S., Johnston, R. & Patel, R. Cloning and expression of a novel enantioselective N-carbobenzyloxy-cleaving enzyme. Enzyme Microb. Technol. 34, 304-312 (2004). (Pubitemid 38186739)
    • (2004) Enzyme and Microbial Technology , vol.34 , Issue.3-4 , pp. 304-312
    • Nanduri, V.B.1    Goldberg, S.2    Johnston, R.3    Patel, R.N.4
  • 25
    • 50049123842 scopus 로고    scopus 로고
    • Tumorigenic activity and therapeutic inhibition of Rheb GTPase
    • Mavrakis, K.J. et al. Tumorigenic activity and therapeutic inhibition of Rheb GTPase. Genes Dev. 22, 2178-2188 (2008).
    • (2008) Genes Dev. , vol.22 , pp. 2178-2188
    • Mavrakis, K.J.1
  • 26
    • 45149083131 scopus 로고    scopus 로고
    • Rapid production of retroviruses for effcient gene delivery to mammalian cells using 293T cell-based systems
    • Swift, S., Lorens, J., Achacoso, P. & Nolan, G.P. Rapid production of retroviruses for effcient gene delivery to mammalian cells using 293T cell-based systems. Curr. Protoc. Immunol. 10, 10.17C (2001).
    • (2001) Curr. Protoc. Immunol. , vol.10
    • Swift, S.1    Lorens, J.2    Achacoso, P.3    Nolan, G.P.4
  • 28
    • 33644872577 scopus 로고    scopus 로고
    • Limma: Linear models for microarray data
    • eds. Gentleman, R., Carey, V., Dudoit, S., Irizarry, R. & Huber, W.) Springer, New York
    • Smyth, G. Limma: linear models for microarray data. in Bioinformatics and Computational Biology Solutions Using R and Bioconductor (eds. Gentleman, R., Carey, V., Dudoit, S., Irizarry, R. & Huber, W.) 397-420 (Springer, New York, 2005).
    • (2005) Bioinformatics and Computational Biology Solutions Using R and Bioconductor , pp. 397-420
    • Smyth, G.1
  • 29
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini, Y. & Hochberg, Y. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J. R. Stat. Soc. B 57, 289-300 (1995).
    • (1995) J. R. Stat. Soc. B , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 31
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J.V. & Mann, M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856-2860 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 32
    • 51649083258 scopus 로고    scopus 로고
    • Phosphorylation of the human full-length protein kinase Ciota
    • Macek, B. et al. Phosphorylation of the human full-length protein kinase Ciota. J. Proteome Res. 7, 2928-2935 (2008).
    • (2008) J. Proteome Res. , vol.7 , pp. 2928-2935
    • MacEk, B.1
  • 33
    • 33645774852 scopus 로고    scopus 로고
    • Modular stop and go extraction tips with stacked disks for parallel and multidimensional Peptide fractionation in proteomics
    • Ishihama, Y., Rappsilber, J. & Mann, M. Modular stop and go extraction tips with stacked disks for parallel and multidimensional Peptide fractionation in proteomics. J. Proteome Res. 5, 988-994 (2006).
    • (2006) J. Proteome Res. , vol.5 , pp. 988-994
    • Ishihama, Y.1    Rappsilber, J.2    Mann, M.3
  • 34
    • 33750456519 scopus 로고    scopus 로고
    • Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
    • DOI 10.1016/j.cell.2006.09.026, PII S0092867406012748
    • Olsen, J.V. et al. Global, in vivo, and site-specifc phosphorylation dynamics in signaling networks. Cell 127, 635-648 (2006). (Pubitemid 44647421)
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 35
    • 79953701087 scopus 로고    scopus 로고
    • Andromeda: A peptide search engine integrated into the MaxQuant environment
    • Cox, J. et al. Andromeda: a peptide search engine integrated into the MaxQuant environment. J. Proteome Res. 10, 1794-1805 (2011).
    • (2011) J. Proteome Res. , vol.10 , pp. 1794-1805
    • Cox, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.