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Volumn 8, Issue 8, 2009, Pages 1908-1920

Systems-wide analysis of a phosphatase knock-down by quantitative proteomics and phosphoproteomics

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; PHOSPHATASE; PHOSPHATASE PTP61F; PHOSPHOPROTEIN; PHOSPHOPROTEOME; PHOSPHOTYROSINE; PROTEIN TYROSINE PHOSPHATASE 1B INHIBITOR; PROTEOME; STABLE ISOTOPE; STAT PROTEIN; STAT92E PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ABI; UNCLASSIFIED DRUG;

EID: 70349621112     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M800559-MCP200     Document Type: Article
Times cited : (86)

References (57)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., and Mann, M. (2003) Mass spectrometry-based proteomics. Nature 422, 198-207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 2
    • 33746730389 scopus 로고    scopus 로고
    • Phosphoproteomic approaches to elucidate cellular signaling networks
    • Schmelzle, K., and White, F. M. (2006) Phosphoproteomic approaches to elucidate cellular signaling networks. Curr. Opin. Biotechnol. 17, 406-414
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 406-414
    • Schmelzle, K.1    White, F.M.2
  • 3
    • 35848970747 scopus 로고    scopus 로고
    • Mapping protein post-translational modifications with mass spectrometry
    • DOI 10.1038/nmeth1100, PII NMETH1100
    • Witze, E. S., Old, W. M., Resing, K. A., and Ahn, N. G. (2007) Mapping protein post-translational modifications with mass spectrometry. Nat. Methods 4, 798-806 (Pubitemid 350055576)
    • (2007) Nature Methods , vol.4 , Issue.10 , pp. 798-806
    • Witze, E.S.1    Old, W.M.2    Resing, K.A.3    Ahn, N.G.4
  • 4
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S. E., and Mann, M. (2005) Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 1, 252-262
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 6
    • 49549116189 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of signaling network dynamics
    • White, F. M. (2008) Quantitative phosphoproteomic analysis of signaling network dynamics. Curr. Opin. Biotechnol. 19, 404-409
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 404-409
    • White, F.M.1
  • 7
    • 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
  • 8
    • 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., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., and Mann, M. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648 (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
  • 9
    • 0035860090 scopus 로고    scopus 로고
    • RNA interference of gene expression (RNAi) in cultured Drosophila cells
    • Worby, C. A., Simonson-Leff, N., and Dixon, J. E. (2001) RNA interference of gene expression (RNAi) in cultured Drosophila cells. Sci. STKE 2001, PL1
    • (2001) Sci. STKE , vol.2001
    • Worby, C.A.1    Simonson-Leff, N.2    Dixon, J.E.3
  • 13
    • 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
  • 14
    • 29144492209 scopus 로고    scopus 로고
    • Involvement of the small protein tyrosine phosphatases TC-PTP and PTP1B in signal transduction and diseases: From diabetes, obesity to cell cycle, and cancer
    • Dubé, N., and Tremblay, M. L. (2005) Involvement of the small protein tyrosine phosphatases TC-PTP and PTP1B in signal transduction and diseases: from diabetes, obesity to cell cycle, and cancer. Biochim. Biophys. Acta 1754, 108-117
    • (2005) Biochim. Biophys. Acta , vol.1754 , pp. 108-117
    • Dubé, N.1    Tremblay, M.L.2
  • 16
    • 23944468103 scopus 로고    scopus 로고
    • Genome-wide RNAi analysis of JAK/STAT signaling components in Drosophila
    • DOI 10.1101/gad.1320705
    • Baeg, G. H., Zhou, R., and Perrimon, N. (2005) Genome-wide RNAi analysis of JAK/STAT signaling components in Drosophila. Genes Dev. 19, 1861-1870 (Pubitemid 41186987)
    • (2005) Genes and Development , vol.19 , Issue.16 , pp. 1861-1870
    • Baeg, G.-H.1    Zhou, R.2    Perrimon, N.3
  • 17
    • 23844483215 scopus 로고    scopus 로고
    • Identification of JAK/STAT signalling components by genome-wide RNA interference
    • DOI 10.1038/nature03869
    • Müller, P., Kuttenkeuler, D., Gesellchen, V., Zeidler, M. P., and Boutros, M. (2005) Identification of JAK/STAT signaling components by genome-wide RNA interference. Nature 436, 871-875 (Pubitemid 41160648)
    • (2005) Nature , vol.436 , Issue.7052 , pp. 871-875
    • Muller, P.1    Kuttenkeuler, D.2    Gesellchen, V.3    Zeidler, M.P.4    Boutros, M.5
  • 18
    • 36148944457 scopus 로고    scopus 로고
    • The involvement of Abl and PTP61F in the regulation of Abi protein localization and stability and lamella formation in Drosophila S2 cells
    • Huang, C. H., Lin, T. Y., Pan, R. L., and Juang, J. L. (2007) The involvement of Abl and PTP61F in the regulation of Abi protein localization and stability and lamella formation in Drosophila S2 cells. J. Biol. Chem. 282, 32442-32452
    • (2007) J. Biol. Chem. , vol.282 , pp. 32442-32452
    • Huang, C.H.1    Lin, T.Y.2    Pan, R.L.3    Juang, J.L.4
  • 20
    • 44449166211 scopus 로고    scopus 로고
    • Tyrosine phosphoproteomics and identification of substrates of protein tyrosine phosphatase dPTP61 F in Drosophila S2 cells by mass spectrometry-based substrate trapping strategy
    • Chang, Y. C., Lin, S. Y., Liang, S. Y., Pan, K. T., Chou, C. C., Chen, C. H., Liao, C. L., Khoo, K. H., and Meng, T. C. (2008) Tyrosine phosphoproteomics and identification of substrates of protein tyrosine phosphatase dPTP61 F in Drosophila S2 cells by mass spectrometry-based substrate trapping strategy. J. Proteome Res. 7, 1055-1066
    • (2008) J. Proteome Res. , vol.7 , pp. 1055-1066
    • Chang, Y.C.1    Lin, S.Y.2    Liang, S.Y.3    Pan, K.T.4    Chou, C.C.5    Chen, C.H.6    Liao, C.L.7    Khoo, K.H.8    Meng, T.C.9
  • 21
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 22
    • 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., and Mann, M. (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856-2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 23
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micropurification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • 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
    • (2007) Nat. Protoc. , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 24
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • 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
    • (2003) Anal. Chem. , vol.75 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 26
    • 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., and Jergensen, T. J. (2005) Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell. Proteomics 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    Jergensen, T.J.5
  • 28
    • 3042824849 scopus 로고    scopus 로고
    • A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry
    • Schroeder, M. J., Shabanowitz, J., Schwartz, J. C., Hunt, D. F., and Coon, J. J. (2004) A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry. Anal. Chem. 76, 3590-3598
    • (2004) Anal. Chem. , vol.76 , pp. 3590-3598
    • Schroeder, M.J.1    Shabanowitz, J.2    Schwartz, J.C.3    Hunt, D.F.4    Coon, J.J.5
  • 29
    • 34547572949 scopus 로고    scopus 로고
    • Is proteomics the new genomics?
    • Cox, J., and Mann, M. (2007) Is proteomics the new genomics? Cell 130, 395-398
    • (2007) Cell , vol.130 , pp. 395-398
    • Cox, J.1    Mann, M.2
  • 30
    • 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
  • 31
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak, K. J., and Schmittgen, T. D. (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 25, 402-408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 32
    • 44149105911 scopus 로고    scopus 로고
    • PHOSIDA (phosphorylation site database): Management, structural and evolutionary investigation, and prediction of phosphosites
    • DOI 10.1186/gb-2007-8-11-r250
    • Gnad, F., Ren, S., Cox, J., Olsen, J. V., Macek, B., Oroshi, M., and Mann, M. (2007) PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites. Genome Biol. 8, R250 (Pubitemid 351917499)
    • (2007) Genome Biology , vol.8 , Issue.11
    • Gnad, F.1    Ren, S.2    Cox, J.3    Olsen, J.V.4    Macek, B.5    Oroshi, M.6    Mann, M.7
  • 33
    • 55849147636 scopus 로고    scopus 로고
    • Quantitative phosphoproteome analysis of a mouse liver cell line reveals specificity of phosphatase inhibitors
    • Pan, C., Gnad, F., Olsen, J. V., and Mann, M. (2008) Quantitative phosphoproteome analysis of a mouse liver cell line reveals specificity of phosphatase inhibitors. Proteomics 8, 4534-4546
    • (2008) Proteomics , vol.8 , pp. 4534-4546
    • Pan, C.1    Gnad, F.2    Olsen, J.V.3    Mann, M.4
  • 34
    • 71049163155 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 35
    • 42649132889 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture (SILAC) and proteome quantitation of mouse embryonic stem cells to a depth of 5,111 proteins
    • Graumann, J., Hubner, N. C., Kim, J. B., Ko, K., Moser, M., Kumar, C., Cox, J., Schöler, H., and Mann, M. (2008) Stable isotope labeling by amino acids in cell culture (SILAC) and proteome quantitation of mouse embryonic stem cells to a depth of 5,111 proteins. Mol. Cell. Proteomics 7, 672-683
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 672-683
    • Graumann, J.1    Hubner, N.C.2    Kim, J.B.3    Ko, K.4    Moser, M.5    Kumar, C.6    Cox, J.7    Schöler, H.8    Mann, M.9
  • 36
    • 0242490780 scopus 로고    scopus 로고
    • Cytoscape: A software Environment for integrated models of biomolecular interaction networks
    • DOI 10.1101/gr.1239303
    • Shannon, P., Markiel, A., Ozier, C., Baliga, N. S., Wang, J. T., Ramage, D., Amin, N., Schwikowski, B., and Ideker, T. (2003) Cytoscape: a software environment for integrated models of biomolecular interaction networks. Genome Res. 13, 2498-2504 (Pubitemid 37428274)
    • (2003) Genome Research , vol.13 , Issue.11 , pp. 2498-2504
    • Shannon, P.1    Markiel, A.2    Ozier, O.3    Baliga, N.S.4    Wang, J.T.5    Ramage, D.6    Amin, N.7    Schwikowski, B.8    Ideker, T.9
  • 37
    • 24044440971 scopus 로고    scopus 로고
    • BiNGO: A Cytoscape plugin to assess overrepresentation of Gene Ontology categories in Biological Networks
    • DOI 10.1093/bioinformatics/bti551
    • Maere, S., Heymans, K., and Kuiper, M. (2005) BiNGO: a Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks. Bioinformatics 21, 3448-3449 (Pubitemid 41222459)
    • (2005) Bioinformatics , vol.21 , Issue.16 , pp. 3448-3449
    • Maere, S.1    Heymans, K.2    Kuiper, M.3
  • 38
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz, D., and Gygi, S. P. (2005) An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat. Biotechnol. 23, 1391-1398
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 41
    • 17844392864 scopus 로고    scopus 로고
    • Combining prediction of secondary structure and solvent accessibility in proteins
    • DOI 10.1002/prot.20441
    • Adamczak, R., Porollo, A., and Meller, J. (2005) Combining prediction of secondary structure and solvent accessibility in proteins. Proteins 59, 467-475 (Pubitemid 40594291)
    • (2005) Proteins: Structure, Function and Genetics , vol.59 , Issue.3 , pp. 467-475
    • Adamczak, R.1    Porollo, A.2    Meller, J.3
  • 42
    • 33644873681 scopus 로고    scopus 로고
    • FlyBase: Anatomical data, images and queries
    • Grumbling, G., and Strelets, V. (2006) FlyBase: anatomical data, images and queries. Nucleic Acids Res. 34, D484-D488
    • (2006) Nucleic Acids Res. , vol.34
    • Grumbling, G.1    Strelets, V.2
  • 45
    • 34547840169 scopus 로고    scopus 로고
    • ProServer: A simple, extensible Perl DAS server
    • DOI 10.1093/bioinformatics/btl650
    • Finn, R. D., Stalker, J. W., Jackson, D. K., Kulesha, E., Clements, J., and Pettett, R. (2007) ProServer: a simple, extensible Perl DAS server. Bioinformatics 23, 1568-1570 (Pubitemid 47244487)
    • (2007) Bioinformatics , vol.23 , Issue.12 , pp. 1568-1570
    • Finn, R.D.1    Stalker, J.W.2    Jackson, D.K.3    Kulesha, E.4    Clements, J.5    Pettett, R.6
  • 46
    • 34248669040 scopus 로고    scopus 로고
    • KaKs-Calculator: Calculating Ka and Ks Through Model Selection and Model Averaging
    • DOI 10.1016/S1672-0229(07)60007-2, PII S1672022907600072
    • Zhang, Z., Li, J., Zhao, X. Q., Wang, J., Wong, G. K., and Yu, J. (2006) KaKs-Calculator: calculating Ka and Ks through model selection and model averaging. Genomic Proteomics Bioinformatics A, 259-263 (Pubitemid 46771391)
    • (2006) Genomics, Proteomics and Bioinformatics , vol.4 , Issue.4 , pp. 259-263
    • Zhang, Z.1    Li, J.2    Zhao, X.-Q.3    Wang, J.4    Wong, G.K.-S.5    Yu, J.6
  • 47
    • 0001514956 scopus 로고    scopus 로고
    • Identification of a Stat gene that functions in Drosophila development
    • Yan, R., Small, S., Desplan, C., Dearolf, C. R., and Darnell, J. E., Jr. (1996) Identification of a Stat gene that functions in Drosophila development. Cell 84, 421-430
    • (1996) Cell , vol.84 , pp. 421-430
    • Yan, R.1    Small, S.2    Desplan, C.3    Dearolf, C.R.4    Darnell Jr., J.E.5
  • 48
    • 33746826011 scopus 로고    scopus 로고
    • JAK/STAT signalling in Drosophila: Insights into conserved regulatory and cellular functions
    • Arbouzova, N. I., and Zeidler, M. P. (2006) JAK/STAT signalling in Drosophila: insights into conserved regulatory and cellular functions. Development 133, 2605-2616
    • (2006) Development , vol.133 , pp. 2605-2616
    • Arbouzova, N.I.1    Zeidler, M.P.2
  • 49
    • 0038445642 scopus 로고    scopus 로고
    • Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases
    • DOI 10.1242/jcs.00622
    • Woodring, P. J., Hunter, T., and Wang, J. Y. (2003) Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases. J. Cell Sci. 116, 2613-2626 (Pubitemid 36857215)
    • (2003) Journal of Cell Science , vol.116 , Issue.13 , pp. 2613-2626
    • Woodring, P.J.1    Hunter, T.2    Wang, J.Y.J.3
  • 50
    • 0023953710 scopus 로고
    • DNA sequence, structure, and tyrosine kinase activity of the Drosophila melanogaster Abelson proto-oncogene homolog
    • Henkemeyer, M. J., Bennett, R. L., Gertler, F. B., and Hoffmann, F. M. (1988) DNA sequence, structure, and tyrosine kinase activity of the Drosophila melanogaster Abelson proto-oncogene homolog. Mol. Cell. Biol. 8, 843-853
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 843-853
    • Henkemeyer, M.J.1    Bennett, R.L.2    Gertler, F.B.3    Hoffmann, F.M.4
  • 51
    • 0037508877 scopus 로고    scopus 로고
    • Two distinct phosphorylation pathways have additive effects on AbI family kinase activation
    • Tanis, K. Q., Veach, D., Duewel, H. S., Bommann, W. G., and Koleske, A. J. (2003) Two distinct phosphorylation pathways have additive effects on AbI family kinase activation. Mol. Cell. Biol. 23, 3884-3896
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3884-3896
    • Tanis, K.Q.1    Veach, D.2    Duewel, H.S.3    Bommann, W.G.4    Koleske, A.J.5
  • 52
    • 0032486386 scopus 로고    scopus 로고
    • Integrins regulate the association and phosphorylation of paxillin by c-Abl
    • Lewis, J. M., and Schwartz, M. A. (1998) Integrins regulate the association and phosphorylation of paxillin by c-Abl. J. Biol. Chem. 273, 14225-14230
    • (1998) J. Biol. Chem. , vol.273 , pp. 14225-14230
    • Lewis, J.M.1    Schwartz, M.A.2
  • 53
    • 0028875460 scopus 로고
    • Increased tyrosine phosphorylation of focal adhesion proteins in myeloid cell lines expressing p210BCR/ABL
    • Salgia, R., Brunkhorst, B., Pisick, E., Li, J. L., Lo, S. H., Chen, L. B., and Griffin, J. D. (1995) Increased tyrosine phosphorylation of focal adhesion proteins in myeloid cell lines expressing p210BCR/ABL. Oncogene 11, 1149-1155
    • (1995) Oncogene , vol.11 , pp. 1149-1155
    • Salgia, R.1    Brunkhorst, B.2    Pisick, E.3    Li, J.L.4    Lo, S.H.5    Chen, L.B.6    Griffin, J.D.7
  • 55
    • 33645713044 scopus 로고    scopus 로고
    • Identification of transcriptional targets associated with the expression of p210 Bcr-Abl
    • Hickey, F. B., and Cotter, T. G. (2006) Identification of transcriptional targets associated with the expression of p210 Bcr-Abl. Eur. J. Haematol. 76, 369-383
    • (2006) Eur. J. Haematol. , vol.76 , pp. 369-383
    • Hickey, F.B.1    Cotter, T.G.2
  • 56
    • 0029589929 scopus 로고
    • The Bcr-Abl leukemia oncogene activates Jun kinase and requires Jun for transformation
    • Raitano, A. B., Halpern, J. R., Hambuch, T. M., and Sawyers, C. L. (1995) The Bcr-Abl leukemia oncogene activates Jun kinase and requires Jun for transformation. Proc. Natl. Acad. Sci. U. S A. 92, 11746-11750
    • (1995) Proc. Natl. Acad. Sci. U. S A. , vol.92 , pp. 11746-11750
    • Raitano, A.B.1    Halpern, J.R.2    Hambuch, T.M.3    Sawyers, C.L.4
  • 57
    • 0026704406 scopus 로고
    • Phorbol ester-induced amino-terminal phosphorylation of human JUN but not JUNB regulates transcriptional activation
    • Franklin, C. C., Sanchez, V., Wagner, F., Woodgett, J. R., and Kraft, A. S. (1992) Phorbol ester-induced amino-terminal phosphorylation of human JUN but not JUNB regulates transcriptional activation. Proc. Natl. Acad. Sci. U. S A. 89, 7247-7251
    • (1992) Proc. Natl. Acad. Sci. U. S A. , vol.89 , pp. 7247-7251
    • Franklin, C.C.1    Sanchez, V.2    Wagner, F.3    Woodgett, J.R.4    Kraft, A.S.5


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