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Volumn 6, Issue 5, 2011, Pages

Phosphoproteomics identifies oncogenic ras signaling targets and their involvement in lung adenocarcinomas

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; APOPTOSIS; ARTICLE; CONTROLLED STUDY; DOWN REGULATION; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION; GENE FUNCTION; GENETIC ANALYSIS; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; LUNG ADENOCARCINOMA; MOLECULAR MECHANICS; ONCOGENE RAS; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEOMICS; RNA PROCESSING; SIGNAL TRANSDUCTION; UPREGULATION; ADENOCARCINOMA; BRONCHUS; CELL LINE; CHEMISTRY; EPITHELIUM CELL; LUNG NON SMALL CELL CANCER; LUNG TUMOR; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; PATHOLOGY; PHOSPHORYLATION; TUMOR CELL LINE;

EID: 79957540957     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0020199     Document Type: Article
Times cited : (32)

References (34)
  • 1
    • 0037264633 scopus 로고    scopus 로고
    • Targeting RAS signalling pathways in cancer therapy
    • Downward J, (2003) Targeting RAS signalling pathways in cancer therapy. Nat Rev Cancer 3: 11-22.
    • (2003) Nat Rev Cancer , vol.3 , pp. 11-22
    • Downward, J.1
  • 3
    • 54549094903 scopus 로고    scopus 로고
    • Somatic mutations affect key pathways in lung adenocarcinoma
    • Ding L, Getz G, Wheeler DA, Mardis ER, McLellan MD, et al. (2008) Somatic mutations affect key pathways in lung adenocarcinoma. Nature 455: 1069-1075.
    • (2008) Nature , vol.455 , pp. 1069-1075
    • Ding, L.1    Getz, G.2    Wheeler, D.A.3    Mardis, E.R.4    McLellan, M.D.5
  • 4
    • 0037805547 scopus 로고    scopus 로고
    • RAS oncogenes: the first 30 years
    • Malumbres M, Barbacid M, (2003) RAS oncogenes: the first 30 years. Nat Rev Cancer 3: 459-465.
    • (2003) Nat Rev Cancer , vol.3 , pp. 459-465
    • Malumbres, M.1    Barbacid, M.2
  • 5
    • 55849105589 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics--an emerging key technology in signal-transduction research
    • Schreiber TB, Mausbacher N, Breitkopf SB, Grundner-Culemann K, Daub H, (2008) Quantitative phosphoproteomics--an emerging key technology in signal-transduction research. Proteomics 8: 4416-4432.
    • (2008) Proteomics , vol.8 , pp. 4416-4432
    • Schreiber, T.B.1    Mausbacher, N.2    Breitkopf, S.B.3    Grundner-Culemann, K.4    Daub, H.5
  • 6
    • 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 AS, Kashyap MK, et al. (2008) Comparisons of tyrosine phosphorylated proteins in cells expressing lung cancer-specific alleles of EGFR and KRAS. Proc Natl Acad Sci U S A 105: 14112-14117.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 14112-14117
    • Guha, U.1    Chaerkady, R.2    Marimuthu, A.3    Patterson, A.S.4    Kashyap, M.K.5
  • 7
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann M, (2006) Functional and quantitative proteomics using SILAC. Nat Rev Mol Cell Biol 7: 952-958.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 952-958
    • Mann, M.1
  • 8
    • 34848822499 scopus 로고    scopus 로고
    • Quantitative profile of five murine core proteomes using label-free functional proteomics
    • Cutillas PR, Vanhaesebroeck B, (2007) Quantitative profile of five murine core proteomes using label-free functional proteomics. Mol Cell Proteomics 6: 1560-1573.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1560-1573
    • Cutillas, P.R.1    Vanhaesebroeck, B.2
  • 9
    • 10844284696 scopus 로고    scopus 로고
    • Immortalization of human bronchial epithelial cells in the absence of viral oncoproteins
    • Ramirez RD, Sheridan S, Girard L, Sato M, Kim Y, et al. (2004) Immortalization of human bronchial epithelial cells in the absence of viral oncoproteins. Cancer Res 64: 9027-9034.
    • (2004) Cancer Res , vol.64 , pp. 9027-9034
    • Ramirez, R.D.1    Sheridan, S.2    Girard, L.3    Sato, M.4    Kim, Y.5
  • 10
    • 33644507072 scopus 로고    scopus 로고
    • Multiple oncogenic changes (K-RAS(V12), p53 knockdown, mutant EGFRs, p16 bypass, telomerase) are not sufficient to confer a full malignant phenotype on human bronchial epithelial cells
    • Sato M, Vaughan MB, Girard L, Peyton M, Lee W, et al. (2006) Multiple oncogenic changes (K-RAS(V12), p53 knockdown, mutant EGFRs, p16 bypass, telomerase) are not sufficient to confer a full malignant phenotype on human bronchial epithelial cells. Cancer Res 66: 2116-2128.
    • (2006) Cancer Res , vol.66 , pp. 2116-2128
    • Sato, M.1    Vaughan, M.B.2    Girard, L.3    Peyton, M.4    Lee, W.5
  • 11
    • 51349126833 scopus 로고    scopus 로고
    • CD44 engagement promotes matrix-derived survival through the CD44-SRC-integrin axis in lipid rafts
    • Lee JL, Wang MJ, Sudhir PR, Chen JY, (2008) CD44 engagement promotes matrix-derived survival through the CD44-SRC-integrin axis in lipid rafts. Molecular and Cellular Biology 28: 5710-5723.
    • (2008) Molecular and Cellular Biology , vol.28 , pp. 5710-5723
    • Lee, J.L.1    Wang, M.J.2    Sudhir, P.R.3    Chen, J.Y.4
  • 12
    • 29244464778 scopus 로고    scopus 로고
    • Tube-gel digestion: a novel proteomic approach for high throughput analysis of membrane proteins
    • Lu X, Zhu H, (2005) Tube-gel digestion: a novel proteomic approach for high throughput analysis of membrane proteins. Mol Cell Proteomics 4: 1948-1958.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1948-1958
    • Lu, X.1    Zhu, H.2
  • 13
    • 55249116044 scopus 로고    scopus 로고
    • Immobilized metal affinity chromatography revisited: pH/acid control toward high selectivity in phosphoproteomics
    • Tsai CF, Wang YT, Chen YR, Lai CY, Lin PY, et al. (2008) Immobilized metal affinity chromatography revisited: pH/acid control toward high selectivity in phosphoproteomics. J Proteome Res 7: 4058-4069.
    • (2008) J Proteome Res , vol.7 , pp. 4058-4069
    • Tsai, C.F.1    Wang, Y.T.2    Chen, Y.R.3    Lai, C.Y.4    Lin, P.Y.5
  • 14
    • 76649139789 scopus 로고    scopus 로고
    • IDEAL-Q, an automated tool for label-free quantitation analysis using an efficient peptide alignment approach and spectral data validation
    • Tsou CC, Tsai CF, Tsui YH, Sudhir PR, Wang YT, et al. (2010) IDEAL-Q, an automated tool for label-free quantitation analysis using an efficient peptide alignment approach and spectral data validation. Mol Cell Proteomics 9: 131-144.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 131-144
    • Tsou, C.C.1    Tsai, C.F.2    Tsui, Y.H.3    Sudhir, P.R.4    Wang, Y.T.5
  • 15
  • 16
    • 0029989103 scopus 로고    scopus 로고
    • An analysis of statistical term strength and its use in the indexing and retrieval of molecular biology texts
    • Wilbur WJ, Yang Y, (1996) An analysis of statistical term strength and its use in the indexing and retrieval of molecular biology texts. Computers in Biology and Medicine 26: 209-222.
    • (1996) Computers in Biology and Medicine , vol.26 , pp. 209-222
    • Wilbur, W.J.1    Yang, Y.2
  • 18
    • 70549087467 scopus 로고    scopus 로고
    • GAP: A graphical environment for matrix visualization and cluster analysis
    • Wu H, Tein Y, Chen C, (2009) GAP: A graphical environment for matrix visualization and cluster analysis. Computational Statistics & Data Analysis 54: 767-778.
    • (2009) Computational Statistics & Data Analysis , vol.54 , pp. 767-778
    • Wu, H.1    Tein, Y.2    Chen, C.3
  • 19
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz D, Gygi SP, (2005) An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nature Biotechnology 23: 1391-1398.
    • (2005) Nature Biotechnology , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 22
    • 67849106825 scopus 로고    scopus 로고
    • Phosphorylation dynamics during early differentiation of human embryonic stem cells
    • Van Hoof D, Munoz J, Braam SR, Pinkse MW, Linding R, et al. (2009) Phosphorylation dynamics during early differentiation of human embryonic stem cells. Cell Stem Cell 5: 214-226.
    • (2009) Cell Stem Cell , vol.5 , pp. 214-226
    • Van Hoof, D.1    Munoz, J.2    Braam, S.R.3    Pinkse, M.W.4    Linding, R.5
  • 23
    • 0027959781 scopus 로고
    • Identification of multiple, novel, protein kinase C-related gene products
    • Palmer RH, Ridden J, Parker PJ, (1994) Identification of multiple, novel, protein kinase C-related gene products. FEBS Letters 356: 5-8.
    • (1994) FEBS Letters , vol.356 , pp. 5-8
    • Palmer, R.H.1    Ridden, J.2    Parker, P.J.3
  • 25
    • 54249115942 scopus 로고    scopus 로고
    • Semaphorin 3B inhibits the phosphatidylinositol 3-kinase/Akt pathway through neuropilin-1 in lung and breast cancer cells
    • Castro-Rivera E, Ran S, Brekken RA, Minna JD, (2008) Semaphorin 3B inhibits the phosphatidylinositol 3-kinase/Akt pathway through neuropilin-1 in lung and breast cancer cells. Cancer Res 68: 8295-8303.
    • (2008) Cancer Res , vol.68 , pp. 8295-8303
    • Castro-Rivera, E.1    Ran, S.2    Brekken, R.A.3    Minna, J.D.4
  • 26
    • 70349795274 scopus 로고    scopus 로고
    • Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport
    • Kosako H, Yamaguchi N, Aranami C, Ushiyama M, Kose S, et al. (2009) Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport. Nat Struct Mol Biol 16: 1026-1035.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 1026-1035
    • Kosako, H.1    Yamaguchi, N.2    Aranami, C.3    Ushiyama, M.4    Kose, S.5
  • 27
    • 63649083462 scopus 로고    scopus 로고
    • Functional proteomics identifies targets of phosphorylation by B-Raf signaling in melanoma
    • Old WM, Shabb JB, Houel S, Wang H, Couts KL, et al. (2009) Functional proteomics identifies targets of phosphorylation by B-Raf signaling in melanoma. Molecular Cell 34: 115-131.
    • (2009) Molecular Cell , vol.34 , pp. 115-131
    • Old, W.M.1    Shabb, J.B.2    Houel, S.3    Wang, H.4    Couts, K.L.5
  • 28
    • 30944447568 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions
    • Yoon S, Seger R, (2006) The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions. Growth Factors 24: 21-44.
    • (2006) Growth Factors , vol.24 , pp. 21-44
    • Yoon, S.1    Seger, R.2
  • 29
    • 65349107082 scopus 로고    scopus 로고
    • KRAS mutations in non-small cell lung cancer
    • Riely GJ, Marks J, Pao W, (2009) KRAS mutations in non-small cell lung cancer. Proc Am Thorac Soc 6: 201-205.
    • (2009) Proc Am Thorac Soc , vol.6 , pp. 201-205
    • Riely, G.J.1    Marks, J.2    Pao, W.3
  • 30
    • 42649125571 scopus 로고    scopus 로고
    • Differential effects of oncogenic K-Ras and N-Ras on proliferation, differentiation and tumor progression in the colon
    • Haigis KM, Kendall KR, Wang Y, Cheung A, Haigis MC, et al. (2008) Differential effects of oncogenic K-Ras and N-Ras on proliferation, differentiation and tumor progression in the colon. Nature Genetics 40: 600-608.
    • (2008) Nature Genetics , vol.40 , pp. 600-608
    • Haigis, K.M.1    Kendall, K.R.2    Wang, Y.3    Cheung, A.4    Haigis, M.C.5
  • 31
    • 0033546419 scopus 로고    scopus 로고
    • Four human ras homologs differ in their abilities to activate Raf-1, induce transformation, and stimulate cell motility
    • Voice JK, Klemke RL, Le A, Jackson JH, (1999) Four human ras homologs differ in their abilities to activate Raf-1, induce transformation, and stimulate cell motility. Journal of Biological Chemistry 274: 17164-17170.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 17164-17170
    • Voice, J.K.1    Klemke, R.L.2    Le, A.3    Jackson, J.H.4
  • 32
    • 0031737627 scopus 로고    scopus 로고
    • Signal transduction as a drug-discovery platform
    • Persidis A, (1998) Signal transduction as a drug-discovery platform. Nature Biotechnology 16: 1082-1083.
    • (1998) Nature Biotechnology , vol.16 , pp. 1082-1083
    • Persidis, A.1
  • 33
    • 65249161129 scopus 로고    scopus 로고
    • Pathway-based biomarker search by high-throughput proteomics profiling of secretomes
    • Lawlor K, Nazarian A, Lacomis L, Tempst P, Villanueva J, (2009) Pathway-based biomarker search by high-throughput proteomics profiling of secretomes. J Proteome Res 8: 1489-1503.
    • (2009) J Proteome Res , vol.8 , pp. 1489-1503
    • Lawlor, K.1    Nazarian, A.2    Lacomis, L.3    Tempst, P.4    Villanueva, J.5


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