메뉴 건너뛰기




Volumn 15, Issue 2-3, 2015, Pages 340-355

Identifying novel targets of oncogenic EGF receptor signaling in lung cancer through global phosphoproteomics

Author keywords

Autophagy; EGFR; Erlotinib; Mass spectrometry; NSCLC; Phosphoproteomics; SILAC

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; CASEIN KINASE; EPIDERMAL GROWTH FACTOR RECEPTOR; ERLOTINIB; INSULIN RECEPTOR; JANUS KINASE; MAMMALIAN TARGET OF RAPAMYCIN; MITOGEN ACTIVATED PROTEIN KINASE; S6 KINASE; SCATTER FACTOR; STAT PROTEIN; PHOSPHOPEPTIDE; PROTEIN KINASE INHIBITOR; QUINAZOLINE DERIVATIVE;

EID: 84921262801     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201400315     Document Type: Article
Times cited : (36)

References (58)
  • 2
    • 2342471392 scopus 로고    scopus 로고
    • Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib
    • Lynch, T. J., Bell, D. W., Sordella, R., Gurubhagavatula, S. et al., Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib. N. Engl. J. Med. 2004, 350, 2129-2139.
    • (2004) N. Engl. J. Med. , vol.350 , pp. 2129-2139
    • Lynch, T.J.1    Bell, D.W.2    Sordella, R.3    Gurubhagavatula, S.4
  • 3
    • 2342624080 scopus 로고    scopus 로고
    • EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy
    • Paez, J. G., Janne, P. A., Lee, J. C., Tracy, S. et al., EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy. Science 2004, 304, 1497-1500.
    • (2004) Science , vol.304 , pp. 1497-1500
    • Paez, J.G.1    Janne, P.A.2    Lee, J.C.3    Tracy, S.4
  • 4
    • 4444344330 scopus 로고    scopus 로고
    • EGF receptor gene mutations are common in lung cancers from "never smokers" and are associated with sensitivity of tumors to gefitinib and erlotinib
    • Pao, W., Miller, V., Zakowski, M., Doherty, J. et al., EGF receptor gene mutations are common in lung cancers from "never smokers" and are associated with sensitivity of tumors to gefitinib and erlotinib. Proc. Natl. Acad. Sci. USA 2004, 101, 13306-13311.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13306-13311
    • Pao, W.1    Miller, V.2    Zakowski, M.3    Doherty, J.4
  • 5
    • 18244371651 scopus 로고    scopus 로고
    • Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain
    • Pao, W., Miller, V. A., Politi, K. A., Riely, G. J. et al., Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain. PLoS Med. 2005, 2, e73.
    • (2005) PLoS Med. , vol.2 , pp. e73
    • Pao, W.1    Miller, V.A.2    Politi, K.A.3    Riely, G.J.4
  • 6
    • 13844317894 scopus 로고    scopus 로고
    • EGFR mutation and resistance of non-small-cell lung cancer to gefitinib
    • Kobayashi, S., Boggon, T. J., Dayaram, T., Janne, P. A. et al., EGFR mutation and resistance of non-small-cell lung cancer to gefitinib. N. Engl. J. Med. 2005, 352, 786-792.
    • (2005) N. Engl. J. Med. , vol.352 , pp. 786-792
    • Kobayashi, S.1    Boggon, T.J.2    Dayaram, T.3    Janne, P.A.4
  • 7
    • 79952711946 scopus 로고    scopus 로고
    • Acquired resistance to EGFR tyrosine kinase inhibitors in EGFR-mutant lung cancer: distinct natural history of patients with tumors harboring the T790M mutation
    • Oxnard, G. R., Arcila, M. E., Sima, C. S., Riely, G. J. et al., Acquired resistance to EGFR tyrosine kinase inhibitors in EGFR-mutant lung cancer: distinct natural history of patients with tumors harboring the T790M mutation. Clin. Cancer Res. 2011, 17, 1616-1622.
    • (2011) Clin. Cancer Res. , vol.17 , pp. 1616-1622
    • Oxnard, G.R.1    Arcila, M.E.2    Sima, C.S.3    Riely, G.J.4
  • 8
    • 33749435816 scopus 로고    scopus 로고
    • Allelic dilution obscures detection of a biologically significant resistance mutation in EGFR-amplified lung cancer
    • Engelman, J. A., Mukohara, T., Zejnullahu, K., Lifshits, E. et al., Allelic dilution obscures detection of a biologically significant resistance mutation in EGFR-amplified lung cancer. J. Clin. Invest. 2006, 116, 2695-2706.
    • (2006) J. Clin. Invest. , vol.116 , pp. 2695-2706
    • Engelman, J.A.1    Mukohara, T.2    Zejnullahu, K.3    Lifshits, E.4
  • 9
    • 4143066760 scopus 로고    scopus 로고
    • Gefitinib-sensitizing EGFR mutations in lung cancer activate anti-apoptotic pathways
    • Sordella, R., Bell, D. W., Haber, D. A., Settleman, J., Gefitinib-sensitizing EGFR mutations in lung cancer activate anti-apoptotic pathways. Science 2004, 305, 1163-1167.
    • (2004) Science , vol.305 , pp. 1163-1167
    • Sordella, R.1    Bell, D.W.2    Haber, D.A.3    Settleman, J.4
  • 10
    • 33750627972 scopus 로고    scopus 로고
    • A common signaling cascade may underlie "addiction" to the Src, BCR-ABL, and EGF receptor oncogenes
    • Sharma, S. V., Gajowniczek, P., Way, I. P., Lee, D. Y. et al., A common signaling cascade may underlie "addiction" to the Src, BCR-ABL, and EGF receptor oncogenes. Cancer Cell 2006, 10, 425-435.
    • (2006) Cancer Cell , vol.10 , pp. 425-435
    • Sharma, S.V.1    Gajowniczek, P.2    Way, I.P.3    Lee, D.Y.4
  • 11
    • 33746388176 scopus 로고    scopus 로고
    • "Oncogenic shock": explaining oncogene addiction through differential signal attenuation
    • Sharma, S. V., Fischbach, M. A., Haber, D. A., Settleman, J., "Oncogenic shock": explaining oncogene addiction through differential signal attenuation. Clin. Cancer Res. 2006, 12, 4392s-4395s.
    • (2006) Clin. Cancer Res. , vol.12 , pp. 4392s-4395s
    • Sharma, S.V.1    Fischbach, M.A.2    Haber, D.A.3    Settleman, J.4
  • 12
    • 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
  • 13
    • 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
  • 14
    • 26844576371 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules
    • Zhang, Y., Wolf-Yadlin, A., Ross, P. L., Pappin, D. J. et al., Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol. Cell. Proteomics 2005, 4, 1240-1250.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1240-1250
    • Zhang, Y.1    Wolf-Yadlin, A.2    Ross, P.L.3    Pappin, D.J.4
  • 15
    • 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
  • 16
    • 84904118558 scopus 로고    scopus 로고
    • Proteomic analysis of the epidermal growth factor receptor (EGFR) interactome and post-translational modifications associated with receptor endocytosis in response to EGF and stress
    • Tong, J., Taylor, P., Moran, M. F., Proteomic analysis of the epidermal growth factor receptor (EGFR) interactome and post-translational modifications associated with receptor endocytosis in response to EGF and stress. Mol. Cell. Proteomics 2014, 13, 1644-1658.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 1644-1658
    • Tong, J.1    Taylor, P.2    Moran, M.F.3
  • 17
    • 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
  • 18
  • 19
    • 84864603830 scopus 로고    scopus 로고
    • EGFR S1166 phosphorylation induced by a combination of EGF and gefitinib has a potentially negative impact on lung cancer cell growth
    • Assiddiq, B. F., Tan, K. Y., Toy, W., Chan, S. P. et al., EGFR S1166 phosphorylation induced by a combination of EGF and gefitinib has a potentially negative impact on lung cancer cell growth. J. Proteome Res. 2012, 11, 4110-4119.
    • (2012) J. Proteome Res. , vol.11 , pp. 4110-4119
    • Assiddiq, B.F.1    Tan, K.Y.2    Toy, W.3    Chan, S.P.4
  • 20
    • 84862907046 scopus 로고    scopus 로고
    • Temporal resolution of autophosphorylation for normal and oncogenic forms of EGFR and differential effects of gefitinib
    • Kim, Y., Li, Z., Apetri, M., Luo, B. et al., Temporal resolution of autophosphorylation for normal and oncogenic forms of EGFR and differential effects of gefitinib. Biochemistry 2012, 51, 5212-5222.
    • (2012) Biochemistry , vol.51 , pp. 5212-5222
    • Kim, Y.1    Li, Z.2    Apetri, M.3    Luo, B.4
  • 21
    • 79951521007 scopus 로고    scopus 로고
    • Mass spectrometry mapping of epidermal growth factor receptor phosphorylation related to oncogenic mutations and tyrosine kinase inhibitor sensitivity
    • Zhang, G., Fang, B., Liu, R. Z., Lin, H. et al., Mass spectrometry mapping of epidermal growth factor receptor phosphorylation related to oncogenic mutations and tyrosine kinase inhibitor sensitivity. J. Proteome Res. 2011, 10, 305-319.
    • (2011) J. Proteome Res. , vol.10 , pp. 305-319
    • Zhang, G.1    Fang, B.2    Liu, R.Z.3    Lin, H.4
  • 22
    • 52949123622 scopus 로고    scopus 로고
    • Comparisons of tyrosine phosphorylated proteins in cells expressing lung cancer-specific alleles of EGFR and KRAS
    • Guha, U., Chaerkady, R., Marimuthu, A., Patterson, A. S. et al., Comparisons of tyrosine phosphorylated proteins in cells expressing lung cancer-specific alleles of EGFR and KRAS. Proc. Natl. Acad. Sci. USA 2008, 105, 14112-14117.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 14112-14117
    • Guha, U.1    Chaerkady, R.2    Marimuthu, A.3    Patterson, A.S.4
  • 23
    • 40649095957 scopus 로고    scopus 로고
    • Quantitative proteomics using stable isotope labeling with amino acids in cell culture
    • Harsha, H. C., Molina, H., Pandey, A., Quantitative proteomics using stable isotope labeling with amino acids in cell culture. Nat. Protoc. 2008, 3, 505-516.
    • (2008) Nat. Protoc. , vol.3 , pp. 505-516
    • Harsha, H.C.1    Molina, H.2    Pandey, A.3
  • 24
    • 84862317369 scopus 로고    scopus 로고
    • TSLP signaling network revealed by SILAC-based phosphoproteomics
    • M112 017764
    • Zhong, J., Kim, M. S., Chaerkady, R., Wu, X. et al., TSLP signaling network revealed by SILAC-based phosphoproteomics. Mol. Cell. Proteomics 2012, 11, M112 017764.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Zhong, J.1    Kim, M.S.2    Chaerkady, R.3    Wu, X.4
  • 25
    • 59149090911 scopus 로고    scopus 로고
    • Strong cation exchange-based fractionation of Lys-N-generated peptides facilitates the targeted analysis of post-translational modifications
    • Taouatas, N., Altelaar, A. F., Drugan, M. M., Helbig, A. O. et al., Strong cation exchange-based fractionation of Lys-N-generated peptides facilitates the targeted analysis of post-translational modifications. Mol. Cell. Proteomics 2009, 8, 190-200.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 190-200
    • Taouatas, N.1    Altelaar, A.F.2    Drugan, M.M.3    Helbig, A.O.4
  • 26
    • 80052347844 scopus 로고    scopus 로고
    • A protocol on the use of titanium dioxide chromatography for phosphoproteomics
    • Pinkse, M. W., Lemeer, S., Heck, A. J., A protocol on the use of titanium dioxide chromatography for phosphoproteomics. Methods Mol. Biol. 2011, 753, 215-228.
    • (2011) Methods Mol. Biol. , vol.753 , pp. 215-228
    • Pinkse, M.W.1    Lemeer, S.2    Heck, A.J.3
  • 27
    • 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
  • 28
    • 34248640261 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides using titanium dioxide
    • Thingholm, T. E., Jorgensen, T. J., Jensen, O. N., Larsen, M. R., Highly selective enrichment of phosphorylated peptides using titanium dioxide. Nat. Protoc. 2006, 1, 1929-1935.
    • (2006) Nat. Protoc. , vol.1 , pp. 1929-1935
    • Thingholm, T.E.1    Jorgensen, T.J.2    Jensen, O.N.3    Larsen, M.R.4
  • 29
    • 79953701087 scopus 로고    scopus 로고
    • Andromeda: a peptide search engine integrated into the MaxQuant environment
    • Cox, J., Neuhauser, N., Michalski, A., Scheltema, R. A. et al., Andromeda: a peptide search engine integrated into the MaxQuant environment. J. Proteome Res. 2011, 10, 1794-1805.
    • (2011) J. Proteome Res. , vol.10 , pp. 1794-1805
    • Cox, J.1    Neuhauser, N.2    Michalski, A.3    Scheltema, R.A.4
  • 30
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • Hornbeck, P. V., Kornhauser, J. M., Tkachev, S., Zhang, B. et al., PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 2012, 40, D261-D270.
    • (2012) Nucleic Acids Res. , vol.40 , pp. D261-D270
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4
  • 31
    • 52649145895 scopus 로고    scopus 로고
    • GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy
    • Xue, Y., Ren, J., Gao, X., Jin, C. et al., GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy. Mol. Cell. Proteomics 2008, 7, 1598-1608.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1598-1608
    • Xue, Y.1    Ren, J.2    Gao, X.3    Jin, C.4
  • 32
    • 18744429842 scopus 로고    scopus 로고
    • Hitting the target: emerging technologies in the search for kinase substrates
    • Manning, B. D., Cantley, L. C., Hitting the target: emerging technologies in the search for kinase substrates. Sci. STKE 2002, 2002, PE49.
    • (2002) Sci. STKE , vol.2002 , pp. PE49
    • Manning, B.D.1    Cantley, L.C.2
  • 33
    • 84885099789 scopus 로고    scopus 로고
    • Kinome Render: a stand-alone and web-accessible tool to annotate the human protein kinome tree
    • Chartier, M., Chenard, T., Barker, J., Najmanovich, R., Kinome Render: a stand-alone and web-accessible tool to annotate the human protein kinome tree. PeerJ 2013, 1, e126.
    • (2013) PeerJ , vol.1 , pp. e126
    • Chartier, M.1    Chenard, T.2    Barker, J.3    Najmanovich, R.4
  • 34
    • 5644293135 scopus 로고    scopus 로고
    • Gefitinib induces apoptosis in the EGFRL858R non-small-cell lung cancer cell line H3255
    • Tracy, S., Mukohara, T., Hansen, M., Meyerson, M. et al., Gefitinib induces apoptosis in the EGFRL858R non-small-cell lung cancer cell line H3255. Cancer Res. 2004, 64, 7241-7244.
    • (2004) Cancer Res. , vol.64 , pp. 7241-7244
    • Tracy, S.1    Mukohara, T.2    Hansen, M.3    Meyerson, M.4
  • 35
    • 79951784508 scopus 로고    scopus 로고
    • Motif-All: discovering all phosphorylation motifs
    • He, Z., Yang, C., Guo, G., Li, N., Yu, W., Motif-All: discovering all phosphorylation motifs. BMC Bioinformatics 2011, 12(Suppl 1), S22.
    • (2011) BMC Bioinformatics , vol.12 , pp. S22
    • He, Z.1    Yang, C.2    Guo, G.3    Li, N.4    Yu, W.5
  • 36
    • 0034680838 scopus 로고    scopus 로고
    • Peptide and protein library screening defines optimal substrate motifs for AKT/PKB
    • Obata, T., Yaffe, M. B., Leparc, G. G., Piro, E. T. et al., Peptide and protein library screening defines optimal substrate motifs for AKT/PKB. J. Biol. Chem. 2000, 275, 36108-36115.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36108-36115
    • Obata, T.1    Yaffe, M.B.2    Leparc, G.G.3    Piro, E.T.4
  • 37
    • 0027585031 scopus 로고
    • Targets of cyclin-dependent protein kinases
    • Nigg, E. A., Targets of cyclin-dependent protein kinases. Curr. Opin. Cell Biol. 1993, 5, 187-193.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 187-193
    • Nigg, E.A.1
  • 38
    • 33846316306 scopus 로고    scopus 로고
    • Quantitative analysis of Akt phosphorylation and activity in response to EGF and insulin treatment
    • Kumar, N., Afeyan, R., Sheppard, S., Harms, B., Lauffenburger, D. A., Quantitative analysis of Akt phosphorylation and activity in response to EGF and insulin treatment. Biochem. Biophys. Res. Commun. 2007, 354, 14-20.
    • (2007) Biochem. Biophys. Res. Commun. , vol.354 , pp. 14-20
    • Kumar, N.1    Afeyan, R.2    Sheppard, S.3    Harms, B.4    Lauffenburger, D.A.5
  • 39
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov, D. D., Guertin, D. A., Ali, S. M., Sabatini, D. M., Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 2005, 307, 1098-1101.
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 40
    • 34347220473 scopus 로고    scopus 로고
    • Defining the role of mTOR in cancer
    • Guertin, D. A., Sabatini, D. M., Defining the role of mTOR in cancer. Cancer Cell 2007, 12, 9-22.
    • (2007) Cancer Cell , vol.12 , pp. 9-22
    • Guertin, D.A.1    Sabatini, D.M.2
  • 41
    • 0033153166 scopus 로고    scopus 로고
    • Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism
    • Gingras, A. C., Gygi, S. P., Raught, B., Polakiewicz, R. D. et al., Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism. Genes Dev. 1999, 13, 1422-1437.
    • (1999) Genes Dev. , vol.13 , pp. 1422-1437
    • Gingras, A.C.1    Gygi, S.P.2    Raught, B.3    Polakiewicz, R.D.4
  • 42
    • 0035498939 scopus 로고    scopus 로고
    • Hierarchical phosphorylation of the translation inhibitor 4E-BP1
    • Gingras, A. C., Raught, B., Gygi, S. P., Niedzwiecka, A. et al., Hierarchical phosphorylation of the translation inhibitor 4E-BP1. Genes Dev. 2001, 15, 2852-2864.
    • (2001) Genes Dev. , vol.15 , pp. 2852-2864
    • Gingras, A.C.1    Raught, B.2    Gygi, S.P.3    Niedzwiecka, A.4
  • 43
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg, N., Hinnebusch, A. G., Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 2009, 136, 731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 44
    • 33745150462 scopus 로고    scopus 로고
    • Ribosomal protein S6 phosphorylation: from protein synthesis to cell size
    • Ruvinsky, I., Meyuhas, O., Ribosomal protein S6 phosphorylation: from protein synthesis to cell size. Trends Biochem. Sci. 2006, 31, 342-348.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 342-348
    • Ruvinsky, I.1    Meyuhas, O.2
  • 45
    • 0037443030 scopus 로고    scopus 로고
    • Altered protein kinase C (PKC) isoforms in non-small cell lung cancer cells: PKCdelta promotes cellular survival and chemotherapeutic resistance
    • Clark, A. S., West, K. A., Blumberg, P. M., Dennis, P. A., Altered protein kinase C (PKC) isoforms in non-small cell lung cancer cells: PKCdelta promotes cellular survival and chemotherapeutic resistance. Cancer Res. 2003, 63, 780-786.
    • (2003) Cancer Res. , vol.63 , pp. 780-786
    • Clark, A.S.1    West, K.A.2    Blumberg, P.M.3    Dennis, P.A.4
  • 46
    • 70350521683 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 4E binding protein family of proteins: sentinels at a translational control checkpoint in lung tumor defense
    • Kim, Y. Y., Von Weymarn, L., Larsson, O., Fan, D. et al., Eukaryotic initiation factor 4E binding protein family of proteins: sentinels at a translational control checkpoint in lung tumor defense. Cancer Res. 2009, 69, 8455-8462.
    • (2009) Cancer Res. , vol.69 , pp. 8455-8462
    • Kim, Y.Y.1    Von Weymarn, L.2    Larsson, O.3    Fan, D.4
  • 47
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends, C., Sowa, M. E., Gygi, S. P., Harper, J. W., Network organization of the human autophagy system. Nature 2010, 466, 68-76.
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 48
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin, V., McEwan, D. G., Novak, I., Dikic, I., A role for ubiquitin in selective autophagy. Mol. Cell 2009, 34, 259-269.
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 49
    • 84905498876 scopus 로고    scopus 로고
    • Tyrosine phosphoproteomics identifies both codrivers and cotargeting strategies for T790M-related EGFR-TKI resistance in non-small cell lung cancer
    • Yoshida, T., Zhang, G., Smith, M. A., Lopez, A. S. et al., Tyrosine phosphoproteomics identifies both codrivers and cotargeting strategies for T790M-related EGFR-TKI resistance in non-small cell lung cancer. Clin. Cancer Res. 2014, 20, 4059-4074.
    • (2014) Clin. Cancer Res. , vol.20 , pp. 4059-4074
    • Yoshida, T.1    Zhang, G.2    Smith, M.A.3    Lopez, A.S.4
  • 50
    • 84892606405 scopus 로고    scopus 로고
    • Phosphoproteomic profiling identifies focal adhesion kinase as a mediator of docetaxel resistance in castrate-resistant prostate cancer
    • Lee, B. Y., Hochgrafe, F., Lin, H. M., Castillo, L. et al., Phosphoproteomic profiling identifies focal adhesion kinase as a mediator of docetaxel resistance in castrate-resistant prostate cancer. Mol. Cancer Ther. 2014, 13, 190-201.
    • (2014) Mol. Cancer Ther. , vol.13 , pp. 190-201
    • Lee, B.Y.1    Hochgrafe, F.2    Lin, H.M.3    Castillo, L.4
  • 51
    • 84855874661 scopus 로고    scopus 로고
    • Dual phosphoproteomics and chemical proteomics analysis of erlotinib and gefitinib interference in acute myeloid leukemia cells
    • Weber, C., Schreiber, T. B., Daub, H., Dual phosphoproteomics and chemical proteomics analysis of erlotinib and gefitinib interference in acute myeloid leukemia cells. J. Proteomics 2012, 75, 1343-1356.
    • (2012) J. Proteomics , vol.75 , pp. 1343-1356
    • Weber, C.1    Schreiber, T.B.2    Daub, H.3
  • 52
    • 84878628963 scopus 로고    scopus 로고
    • Phosphoproteome dynamics reveal novel ERK1/2 MAP kinase substrates with broad spectrum of functions
    • Courcelles, M., Fremin, C., Voisin, L., Lemieux, S. et al., Phosphoproteome dynamics reveal novel ERK1/2 MAP kinase substrates with broad spectrum of functions. Mol. Syst. Biol. 2013, 9, 669.
    • (2013) Mol. Syst. Biol. , vol.9 , pp. 669
    • Courcelles, M.1    Fremin, C.2    Voisin, L.3    Lemieux, S.4
  • 53
    • 43649104356 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 phosphorylation of human septin SEPT5 (hCDCrel-1) modulates exocytosis
    • Amin, N. D., Zheng, Y. L., Kesavapany, S., Kanungo, J. et al., Cyclin-dependent kinase 5 phosphorylation of human septin SEPT5 (hCDCrel-1) modulates exocytosis. J. Neurosci. 2008, 28, 3631-3643.
    • (2008) J. Neurosci. , vol.28 , pp. 3631-3643
    • Amin, N.D.1    Zheng, Y.L.2    Kesavapany, S.3    Kanungo, J.4
  • 54
    • 40349092941 scopus 로고    scopus 로고
    • Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates
    • Blethrow, J. D., Glavy, J. S., Morgan, D. O., Shokat, K. M., Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates. Proc. Natl. Acad. Sci. USA 2008, 105, 1442-1447.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 1442-1447
    • Blethrow, J.D.1    Glavy, J.S.2    Morgan, D.O.3    Shokat, K.M.4
  • 55
    • 0025230741 scopus 로고
    • Differential phosphorylation of c-Abl in cell cycle determined by cdc2 kinase and phosphatase activity
    • Kipreos, E. T., Wang, J. Y., Differential phosphorylation of c-Abl in cell cycle determined by cdc2 kinase and phosphatase activity. Science 1990, 248, 217-220.
    • (1990) Science , vol.248 , pp. 217-220
    • Kipreos, E.T.1    Wang, J.Y.2
  • 56
    • 0028885494 scopus 로고
    • Protein phosphatase 2A is the major enzyme in brain that dephosphorylates tau protein phosphorylated by proline-directed protein kinases or cyclic AMP-dependent protein kinase
    • Goedert, M., Jakes, R., Qi, Z., Wang, J. H., Cohen, P., Protein phosphatase 2A is the major enzyme in brain that dephosphorylates tau protein phosphorylated by proline-directed protein kinases or cyclic AMP-dependent protein kinase. J. Neurochem. 1995, 65, 2804-2807.
    • (1995) J. Neurochem. , vol.65 , pp. 2804-2807
    • Goedert, M.1    Jakes, R.2    Qi, Z.3    Wang, J.H.4    Cohen, P.5
  • 57
    • 33847317020 scopus 로고    scopus 로고
    • Protein kinase A activates protein phosphatase 2A by phosphorylation of the B56delta subunit
    • Ahn, J. H., McAvoy, T., Rakhilin, S. V., Nishi, A. et al., Protein kinase A activates protein phosphatase 2A by phosphorylation of the B56delta subunit. Proc. Natl. Acad. Sci. USA 2007, 104, 2979-2984.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2979-2984
    • Ahn, J.H.1    McAvoy, T.2    Rakhilin, S.V.3    Nishi, A.4
  • 58
    • 84874762979 scopus 로고    scopus 로고
    • The PRoteomics IDEntifications (PRIDE) database and associated tools: status in 2013
    • Vizcaíno, J. A., Côté, R. G., Csordas, A., Dianes, J. A. et al., The PRoteomics IDEntifications (PRIDE) database and associated tools: status in 2013. Nucleic Acids Res 2012, 104, doi: 10.1093/nar/gks1262.
    • (2012) Nucleic Acids Res , vol.104
    • Vizcaíno, J.A.1    Côté, R.G.2    Csordas, A.3    Dianes, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.