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Volumn 2, Issue 8, 2005, Pages 591-598

Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

CD3 ANTIGEN; DENDRIMER; IMIDAZOLE; IMIDE; PHOSPHOPROTEIN; POLYMER; PROTEOME; T LYMPHOCYTE RECEPTOR; TYROSINE;

EID: 23144441172     PISSN: 15487091     EISSN: None     Source Type: Journal    
DOI: 10.1038/nmeth776     Document Type: Article
Times cited : (284)

References (46)
  • 1
    • 0842346438 scopus 로고    scopus 로고
    • Specificity in signal transduction: From phosphotyrosine-SH2 domain interactions to complex cellular systems
    • Pawson, T. Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. Cell 116, 191-203 (2004).
    • (2004) Cell , vol.116 , pp. 191-203
    • Pawson, T.1
  • 3
  • 4
    • 15944373459 scopus 로고    scopus 로고
    • Mass spectrometric contributions to the practice of phosphorylation site mapping through 2003: A literature review
    • Loyet, K.M., Stults, J.T. & Arnott, D. Mass spectrometric contributions to the practice of phosphorylation site mapping through 2003: a literature review. Mol. Cell Proteomics 4, 235-245 (2005).
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 235-245
    • Loyet, K.M.1    Stults, J.T.2    Arnott, D.3
  • 5
    • 4644328163 scopus 로고    scopus 로고
    • Comparative phosphorylation site mapping from gel-derived proteins using a multidimensional ES/MS-based approach
    • Zappacosta, F., Huddleston, M.J. & Annan, R.S. Comparative phosphorylation site mapping from gel-derived proteins using a multidimensional ES/MS-based approach. Methods Mol. Biol. 284, 91-110 (2004).
    • (2004) Methods Mol. Biol. , vol.284 , pp. 91-110
    • Zappacosta, F.1    Huddleston, M.J.2    Annan, R.S.3
  • 6
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: Deciphering the phosphoproteome
    • Mann, M. et al. Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol. 20, 261-268 (2002).
    • (2002) Trends Biotechnol. , vol.20 , pp. 261-268
    • Mann, M.1
  • 7
    • 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. 22, 1139-1145 (2004).
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.E.2    Kratchmarova, I.3    Mann, M.4
  • 8
    • 2442658049 scopus 로고    scopus 로고
    • Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry
    • Brill, L.M. et al. Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Anal. Chem. 76, 2763-2772 (2004).
    • (2004) Anal. Chem. , vol.76 , pp. 2763-2772
    • Brill, L.M.1
  • 9
    • 21144445429 scopus 로고    scopus 로고
    • Phosphotyrosine proteomic study of interferon signaling pathway using a combination of immunoprecipitation and immobilized metal affinity chromatography
    • Zheng, H., Hu, P., Quinn, D.F. & Wang, Y.K. Phosphotyrosine proteomic study of interferon signaling pathway using a combination of immunoprecipitation and immobilized metal affinity chromatography. Mol. Cell. Proteomics 4, 721-730 (2005).
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 721-730
    • Zheng, H.1    Hu, P.2    Quinn, D.F.3    Wang, Y.K.4
  • 10
    • 0034602654 scopus 로고    scopus 로고
    • Analysis of receptor signaling pathways by mass spectrometry: Identification of vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors
    • Pandey, A. et al. Analysis of receptor signaling pathways by mass spectrometry: identification of vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors. Proc. Natl. Acad. Sci. USA 97, 179-184 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 179-184
    • Pandey, A.1
  • 11
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush, J. et al. Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat. Biotechnol. 23, 94-101 (2005).
    • (2005) Nat. Biotechnol. , vol.23 , pp. 94-101
    • Rush, J.1
  • 12
    • 0036198435 scopus 로고    scopus 로고
    • Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae
    • Ficarro, S.B. et al. Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae. Nat. Biotechnol. 20, 301-305 (2002).
    • (2002) Nat. Biotechnol. , vol.20 , pp. 301-305
    • Ficarro, S.B.1
  • 14
    • 0842299091 scopus 로고    scopus 로고
    • Identification of novel phosphorylation sites on Xenopus laevis Aurora A and analysis of phosphopeptide enrichment by immobilized metal-affinity chromatography
    • Haydon, C.E. et al. Identification of novel phosphorylation sites on Xenopus laevis Aurora A and analysis of phosphopeptide enrichment by immobilized metal-affinity chromatography. Mol. Cell. Proteomics 2, 1055-1067 (2003).
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1055-1067
    • Haydon, C.E.1
  • 15
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou, H., Watts, J.D. & Aebersold, R. A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 19, 375-378 (2001).
    • (2001) Nat. Biotechnol. , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 16
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda, Y., Nagasu, T. & Chait, B.T. Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 19, 379-382 (2001).
    • (2001) Nat. Biotechnol. , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 17
    • 0034921817 scopus 로고    scopus 로고
    • Differential stable isotope labeling of peptides for quantitation and de novo sequence derivation
    • Goodlett, D.R. et al. Differential stable isotope labeling of peptides for quantitation and de novo sequence derivation. Rapid Commun. Mass Spectrom. 15, 1214-1221 (2001).
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 1214-1221
    • Goodlett, D.R.1
  • 18
    • 0021111261 scopus 로고
    • Derivatization of unprotected polynucleotides
    • Chu, B., Wahl, G.M. & Orgel, L.E. Derivatization of unprotected polynucleotides. Nucleic Acids Res. 11, 6513-6529 (1983).
    • (1983) Nucleic Acids Res. , vol.11 , pp. 6513-6529
    • Chu, B.1    Wahl, G.M.2    Orgel, L.E.3
  • 19
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S.P. et al. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17, 994-999 (1999).
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1
  • 20
    • 0344737959 scopus 로고    scopus 로고
    • Automated statistical analysis of protein abundance ratios from data generated by stable-isotope dilution and tandem mass spectrometry
    • Li, X., Zhang, H., Ranish, J.A. & Aebersold, R. Automated statistical analysis of protein abundance ratios from data generated by stable-isotope dilution and tandem mass spectrometry. Anal. Chem. 75, 6648-6657 (2003).
    • (2003) Anal. Chem. , vol.75 , pp. 6648-6657
    • Li, X.1    Zhang, H.2    Ranish, J.A.3    Aebersold, R.4
  • 21
    • 0027315182 scopus 로고
    • T cell antigen receptor signal transduction: A tale of tails and cytoplasmic protein-tyrosine kinases
    • Weiss, A. T cell antigen receptor signal transduction: a tale of tails and cytoplasmic protein-tyrosine kinases. Cell 73, 209-212 (1993).
    • (1993) Cell , vol.73 , pp. 209-212
    • Weiss, A.1
  • 22
    • 0037306051 scopus 로고    scopus 로고
    • Initiation of TCR signaling: Regulation within CD3 dimers
    • Alarcon, B., Gil, D., Delgado, P. & Schamel, W.W. Initiation of TCR signaling: regulation within CD3 dimers. Immunol. Rev. 191, 38-46 (2003).
    • (2003) Immunol. Rev. , vol.191 , pp. 38-46
    • Alarcon, B.1    Gil, D.2    Delgado, P.3    Schamel, W.W.4
  • 23
    • 0032885755 scopus 로고    scopus 로고
    • Coupling the TCR to downstream signalling pathways: The role of cytoplasmic and transmembrane adaptor proteins
    • Marie-Cardine, A. & Schraven, B. Coupling the TCR to downstream signalling pathways: the role of cytoplasmic and transmembrane adaptor proteins. Cell. Signal. 11, 705-712 (1999).
    • (1999) Cell. Signal , vol.11 , pp. 705-712
    • Marie-Cardine, A.1    Schraven, B.2
  • 24
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A.I., Keller, A., Kolker, E. & Aebersold, R. A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 75, 4646-4658 (2003).
    • (2003) Anal. Chem. , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 25
    • 0029992806 scopus 로고    scopus 로고
    • Combinatorial chemistry: A liquid-phase approach
    • Janda, K.D. & Han, H. Combinatorial chemistry: a liquid-phase approach. Methods Enzymol. 267, 234-247 (1996).
    • (1996) Methods Enzymol. , vol.267 , pp. 234-247
    • Janda, K.D.1    Han, H.2
  • 26
    • 0036810318 scopus 로고    scopus 로고
    • Dendrimers as support for recoverable catalysts and reagents
    • van Heerbeek, R., Kamer, P.C., van Leeuwen, P.W. & Reek, J.N. Dendrimers as support for recoverable catalysts and reagents. Chem. Rev. 102, 3717-3756 (2002).
    • (2002) Chem. Rev. , vol.102 , pp. 3717-3756
    • van Heerbeek, R.1    Kamer, P.C.2    van Leeuwen, P.W.3    Reek, J.N.4
  • 27
    • 0038674868 scopus 로고    scopus 로고
    • About dendrimers: Structure, physical properties and applications
    • Bosman, A.W., Janssen, H.M. & Meijer, E.W. About dendrimers: structure, physical properties and applications. Chem. Rev. 99, 1665-1688 (1999).
    • (1999) Chem. Rev. , vol.99 , pp. 1665-1688
    • Bosman, A.W.1    Janssen, H.M.2    Meijer, E.W.3
  • 28
    • 0029810688 scopus 로고    scopus 로고
    • Dendrimer-supported combinatorial chemistry
    • Kim, R.M. et al. Dendrimer-supported combinatorial chemistry. Proc. Natl. Acad. Sci. USA 93, 10012-10017 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10012-10017
    • Kim, R.M.1
  • 29
    • 0033666867 scopus 로고    scopus 로고
    • ITAM multiplicity and thymocyte selection: How low can you go?
    • Love, P.E. & Shores, E.W. ITAM multiplicity and thymocyte selection: how low can you go? Immunity 12, 591-597 (2000).
    • (2000) Immunity , vol.12 , pp. 591-597
    • Love, P.E.1    Shores, E.W.2
  • 30
    • 0032563231 scopus 로고    scopus 로고
    • Fidelity of T cell activation through multistep T-cell receptor zeta phosphorylation
    • Kersh, E.N., Shaw, A.S. & Allen, P.M. Fidelity of T cell activation through multistep T-cell receptor zeta phosphorylation. Science 281, 572-575 (1998).
    • (1998) Science , vol.281 , pp. 572-575
    • Kersh, E.N.1    Shaw, A.S.2    Allen, P.M.3
  • 31
    • 0037093352 scopus 로고    scopus 로고
    • Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells
    • Ruzzene, M., Penzo, D. & Pinna, L.A. Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells. Biochem. J. 364, 41-47 (2002).
    • (2002) Biochem. J. , vol.364 , pp. 41-47
    • Ruzzene, M.1    Penzo, D.2    Pinna, L.A.3
  • 32
    • 0029847936 scopus 로고    scopus 로고
    • Evidence for a preformed transducer complex organized by the B cell antigen receptor
    • Wienands, J., Larbolette, O. & Reth, M. Evidence for a preformed transducer complex organized by the B cell antigen receptor. Proc. Natl. Acad. Sci. USA 93, 7865-7870 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7865-7870
    • Wienands, J.1    Larbolette, O.2    Reth, M.3
  • 33
    • 0028023767 scopus 로고
    • In vitro characterization of major ligands for Src homology 2 domains derived from protein tyrosine kinases, from the adaptor protein SHC and from GTPase-activating protein in Ramos B cells
    • Baumann, G. et al. In vitro characterization of major ligands for Src homology 2 domains derived from protein tyrosine kinases, from the adaptor protein SHC and from GTPase-activating protein in Ramos B cells. Eur. J. Immunol. 24, 1799-1807 (1994).
    • (1994) Eur. J. Immunol. , vol.24 , pp. 1799-1807
    • Baumann, G.1
  • 34
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J.K., McCormack, A.L. & Yate, J.R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989 (1994).
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yate, J.R.3
  • 35
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., Nesvizhskii, A.I., Kolker, E. & Aebersold, R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 74, 5383-5392 (2002).
    • (2002) Anal. Chem. , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 36
    • 2442474012 scopus 로고    scopus 로고
    • Regulation of cell migration and survival by focal adhesion targeting of Lasp-1
    • Lin, Y.H. et al. Regulation of cell migration and survival by focal adhesion targeting of Lasp-1. J. Cell Biol. 165, 421-432 (2004).
    • (2004) J. Cell Biol. , vol.165 , pp. 421-432
    • Lin, Y.H.1
  • 37
    • 0030028599 scopus 로고    scopus 로고
    • Characterization of ERK1 activation site mutants and the effect on recognition by MEK1 and MEK2
    • Butch, E.R. & Guan, K.L. Characterization of ERK1 activation site mutants and the effect on recognition by MEK1 and MEK2. J. Biol. Chem. 271, 4230-4235 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 4230-4235
    • Butch, E.R.1    Guan, K.L.2
  • 38
    • 0037458030 scopus 로고    scopus 로고
    • Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry
    • Salomon, A.R. et al. Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry. Proc. Natl. Acad. Sci. USA 100, 443-448 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 443-448
    • Salomon, A.R.1
  • 39
    • 0033622043 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of p62dok by p210bcr-abl inhibits RasGAP activity
    • Kashige, N., Carpino, N. & Kobayashi, R. Tyrosine phosphorylation of p62dok by p210bcr-abl inhibits RasGAP activity. Proc. Natl. Acad. Sci. USA 97, 2093-2098 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2093-2098
    • Kashige, N.1    Carpino, N.2    Kobayashi, R.3
  • 40
    • 0030820813 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the CD3-epsilon subunit of the T-cell antigen receptor mediates enhanced association with phosphatidylinositol 3-kinase in Jurkat T cells
    • de Aos, I. et al. Tyrosine phosphorylation of the CD3-epsilon subunit of the T-cell antigen receptor mediates enhanced association with phosphatidylinositol 3-kinase in Jurkat T cells. J. Biol. Chem. 272, 25310-25318 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 25310-25318
    • de Aos, I.1
  • 41
    • 0029910720 scopus 로고    scopus 로고
    • Phosphorylation of each of the distal three tyrosines of the CD28 cytoplasmic tail is required for CD28-induced T cell IL-2 secretion
    • Teng, J.M. et al. Phosphorylation of each of the distal three tyrosines of the CD28 cytoplasmic tail is required for CD28-induced T cell IL-2 secretion. Tissue Antigens 48, 255-264 (1996).
    • (1996) Tissue Antigens , vol.48 , pp. 255-264
    • Teng, J.M.1
  • 42
    • 0038373277 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase SHP-2 regulates interleukin-1-induced ERK activation in fibroblasts
    • MacGillivray, M. et al. The protein tyrosine phosphatase SHP-2 regulates interleukin-1-induced ERK activation in fibroblasts. J. Biol. Chem. 278, 27190-27198 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 27190-27198
    • MacGillivray, M.1
  • 43
    • 0028062116 scopus 로고
    • Identification by electrospray ionization mass spectrometry of the sites of tyrosine phosphorylation induced in activated Jurkat T cells on the protein tyrosine kinase ZAP-70
    • Watts, J.D. et al. Identification by electrospray ionization mass spectrometry of the sites of tyrosine phosphorylation induced in activated Jurkat T cells on the protein tyrosine kinase ZAP-70. J. Biol. Chem. 269, 29520-29529 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 29520-29529
    • Watts, J.D.1
  • 44
    • 0033553463 scopus 로고    scopus 로고
    • Tyrosine 319 in the interdomain B of ZAP-70 is a binding site for the Src homology 2 domain of Lck
    • Pelosi, M. et al. Tyrosine 319 in the interdomain B of ZAP-70 is a binding site for the Src homology 2 domain of Lck. J. Biol. Chem. 274, 14229-14237 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 14229-14237
    • Pelosi, M.1
  • 45
    • 4344574540 scopus 로고    scopus 로고
    • Large-scale characterization of HeLa cell nuclear phosphoproteins
    • Beausoleil, S.A. et al. Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc. Natl. Acad. Sci. USA 101, 12130-12135 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12130-12135
    • Beausoleil, S.A.1
  • 46
    • 3142677813 scopus 로고    scopus 로고
    • Regulation of cytosolic prostaglandin E synthase by phosphorylation
    • Kobayashi, T. et al. Regulation of cytosolic prostaglandin E synthase by phosphorylation. Biochem. J. 381, 59-69 (2004).
    • (2004) Biochem. J. , vol.381 , pp. 59-69
    • Kobayashi, T.1


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