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Volumn 7, Issue 335, 2014, Pages

Time-resolved dissection of early phosphoproteome and ensuing proteome changes in response to TGF-β

Author keywords

[No Author keywords available]

Indexed keywords

ATM PROTEIN; BRG1 PROTEIN; GLYCOGEN SYNTHASE KINASE 3; GUANINE NUCLEOTIDE BINDING PROTEIN; HUNTINGTIN; INTEGRIN; MINICHROMOSOME MAINTENANCE PROTEIN 6; PHOSPHOPROTEOME; PROLINE RICH PROTEIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; PROTEIN KINASE B; PROTEIN P53; PROTEOME; RECOMBINANT SOMATOMEDIN C; SMAD2 PROTEIN; SMAD3 PROTEIN; SMAD4 PROTEIN; SMOOTH MUSCLE ACTIN; TATA BINDING PROTEIN; TRANSFORMING GROWTH FACTOR BETA; TRANSGELIN; UNCLASSIFIED DRUG; VITAMIN D RECEPTOR; PHOSPHOPROTEIN;

EID: 84906841343     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2004856     Document Type: Article
Times cited : (37)

References (127)
  • 1
    • 47549090432 scopus 로고    scopus 로고
    • TGFβ in cancer
    • J. Massagué, TGFβ in cancer. Cell 134, 215-230 (2008).
    • (2008) Cell , vol.134 , pp. 215-230
    • Massagué, J.1
  • 2
    • 0037013742 scopus 로고    scopus 로고
    • Mechanisms of TGF-β signaling in regulation of cell growth and differentiation
    • A. Moustakas, K. Pardali, A. Gaal, C. H. Heldin, Mechanisms of TGF-β signaling in regulation of cell growth and differentiation. Immunol. Lett. 82, 85-91 (2002).
    • (2002) Immunol. Lett. , vol.82 , pp. 85-91
    • Moustakas, A.1    Pardali, K.2    Gaal, A.3    Heldin, C.H.4
  • 3
    • 0034604110 scopus 로고    scopus 로고
    • Mechanisms of disease: Role of transforming growth factor β in human disease
    • G. C. Blobe, W. P. Schiemann, H. F. Lodish, Mechanisms of disease: Role of transforming growth factor β in human disease. N. Engl. J. Med. 342, 1350-1358 (2000).
    • (2000) N. Engl. J. Med. , vol.342 , pp. 1350-1358
    • Blobe, G.C.1    Schiemann, W.P.2    Lodish, H.F.3
  • 4
    • 84866742560 scopus 로고    scopus 로고
    • TGFβ signalling in context
    • J. Massagué, TGFβ signalling in context. Nat. Rev. Mol. Cell Biol. 13, 616-630 (2012).
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 616-630
    • Massagué, J.1
  • 5
    • 67650999875 scopus 로고    scopus 로고
    • The basics of epithelial-mesenchymal transition
    • R. Kalluri, R. A. Weinberg, The basics of epithelial-mesenchymal transition. J. Clin. Invest. 119, 1420-1428 (2009).
    • (2009) J. Clin. Invest. , vol.119 , pp. 1420-1428
    • Kalluri, R.1    Weinberg, R.A.2
  • 6
    • 70349729970 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition and cell cooperativity in metastasis
    • T. Tsuji, S. Ibaragi, G. F. Hu, Epithelial-mesenchymal transition and cell cooperativity in metastasis. Cancer Res. 69, 7135-7139 (2009).
    • (2009) Cancer Res. , vol.69 , pp. 7135-7139
    • Tsuji, T.1    Ibaragi, S.2    Hu, G.F.3
  • 7
    • 84866324123 scopus 로고    scopus 로고
    • Cancer stem cells and epithelial-mesenchymal transition: Concepts and molecular links
    • C. Scheel, R. A. Weinberg, Cancer stem cells and epithelial-mesenchymal transition: Concepts and molecular links. Semin. Cancer Biol. 22, 396-403 (2012).
    • (2012) Semin. Cancer Biol. , vol.22 , pp. 396-403
    • Scheel, C.1    Weinberg, R.A.2
  • 8
    • 0028179175 scopus 로고
    • Induction of α-smooth muscle actin expression in cultured human brain pericytes by transforming growth factor-β 1
    • M. M. Verbeek, I. Otte-Holler, P. Wesseling, D. J. Ruiter, R. M. de Waal, Induction of α-smooth muscle actin expression in cultured human brain pericytes by transforming growth factor-β 1. Am. J. Pathol. 144, 372-382 (1994).
    • (1994) Am. J. Pathol. , vol.144 , pp. 372-382
    • Verbeek, M.M.1    Otte-Holler, I.2    Wesseling, P.3    Ruiter, D.J.4    De Waal, R.M.5
  • 9
    • 0023025366 scopus 로고
    • Transforming growth factor-β stimulates the expression of fibronectin and collagen and their incorporation into the extracellular matrix
    • R. A. Ignotz, J. Massagué, Transforming growth factor-β stimulates the expression of fibronectin and collagen and their incorporation into the extracellular matrix. J. Biol. Chem. 261, 4337-4345 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 4337-4345
    • Ignotz, R.A.1    Massagué, J.2
  • 10
    • 74949093198 scopus 로고    scopus 로고
    • Transforming growth factor-β signaling in epithelial-mesenchymal transition and progression of cancer
    • K. Miyazono, Transforming growth factor-β signaling in epithelial-mesenchymal transition and progression of cancer. Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. 85, 314-323 (2009).
    • (2009) Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. , vol.85 , pp. 314-323
    • Miyazono, K.1
  • 11
    • 33745515023 scopus 로고    scopus 로고
    • Tumour microenvironment: TGFβ: The molecular Jekyll and Hyde of cancer
    • B. Bierie, H. L. Moses, Tumour microenvironment: TGFβ: The molecular Jekyll and Hyde of cancer. Nat. Rev. Cancer 6, 506-520 (2006).
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 506-520
    • Bierie, B.1    Moses, H.L.2
  • 12
    • 0035501062 scopus 로고    scopus 로고
    • TGF-β signaling in cancer - A double-edged sword
    • R. J. Akhurst, R. Derynck, TGF-β signaling in cancer - A double-edged sword. Trends Cell Biol. 11, S44-S51 (2001).
    • (2001) Trends Cell Biol. , vol.11 , pp. S44-S51
    • Akhurst, R.J.1    Derynck, R.2
  • 14
    • 0030300115 scopus 로고    scopus 로고
    • MADR2 is a substrate of the TGFβ receptor and its phosphorylation is required for nuclear accumulation and signaling
    • M. Macías-Silva, S. Abdollah, P. A. Hoodless, R. Pirone, L. Attisano, J. L. Wrana, MADR2 is a substrate of the TGFβ receptor and its phosphorylation is required for nuclear accumulation and signaling. Cell 87, 1215-1224 (1996).
    • (1996) Cell , vol.87 , pp. 1215-1224
    • Macías-Silva, M.1    Abdollah, S.2    Hoodless, P.A.3    Pirone, R.4    Attisano, L.5    Wrana, J.L.6
  • 15
    • 0032428684 scopus 로고    scopus 로고
    • SARA, a FYVE domain protein that recruits Smad2 to the TGFβ receptor
    • T. Tsukazaki, T. A. Chiang, A. F. Davison, L. Attisano, J. L. Wrana, SARA, a FYVE domain protein that recruits Smad2 to the TGFβ receptor. Cell 95, 779-791 (1998).
    • (1998) Cell , vol.95 , pp. 779-791
    • Tsukazaki, T.1    Chiang, T.A.2    Davison, A.F.3    Attisano, L.4    Wrana, J.L.5
  • 16
    • 0029786212 scopus 로고    scopus 로고
    • Receptor-associated Mad homologues synergize as effectors of the TGF-β response
    • Y. Zhang, X. Feng, R. We, R. Derynck, Receptor-associated Mad homologues synergize as effectors of the TGF-β response. Nature 383, 168-172 (1996).
    • (1996) Nature , vol.383 , pp. 168-172
    • Zhang, Y.1    Feng, X.2    We, R.3    Derynck, R.4
  • 17
    • 0029834067 scopus 로고    scopus 로고
    • Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways
    • G. Lagna, A. Hata, A. HemmatiBrivanlou, J. Massagué, Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways. Nature 383, 832-836 (1996).
    • (1996) Nature , vol.383 , pp. 832-836
    • Lagna, G.1    Hata, A.2    HemmatiBrivanlou, A.3    Massagué, J.4
  • 18
    • 0034678908 scopus 로고    scopus 로고
    • Transcriptional control by the TGF-β/Smad signaling system
    • J. Massagué, D. Wotton, Transcriptional control by the TGF-β/Smad signaling system. EMBO J. 19, 1745-1754 (2000).
    • (2000) EMBO J. , vol.19 , pp. 1745-1754
    • Massagué, J.1    Wotton, D.2
  • 19
    • 0033200361 scopus 로고    scopus 로고
    • The Ski oncoprotein interacts with the Smad proteins to repress TGFb signaling
    • K. Luo, S. L. Stroschein, W. Wang, D. Chen, E. Martens, S. Zhou, Q. Zhou, The Ski oncoprotein interacts with the Smad proteins to repress TGFb signaling. Genes Dev. 13, 2196-2206 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2196-2206
    • Luo, K.1    Stroschein, S.L.2    Wang, W.3    Chen, D.4    Martens, E.5    Zhou, S.6    Zhou, Q.7
  • 20
    • 0033521032 scopus 로고    scopus 로고
    • c-Ski acts as a transcriptional co-repressor in transforming growth factor-β signaling through interaction with Smads
    • S. Akiyoshi, H. Inoue, J. Hanai, K. Kusanagi, N. Nemoto, K. Miyazono, M. Kawabata, c-Ski acts as a transcriptional co-repressor in transforming growth factor-β signaling through interaction with Smads. J. Biol. Chem. 274, 35269-35277 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 35269-35277
    • Akiyoshi, S.1    Inoue, H.2    Hanai, J.3    Kusanagi, K.4    Nemoto, N.5    Miyazono, K.6    Kawabata, M.7
  • 21
    • 0034703083 scopus 로고    scopus 로고
    • Role of Smad proteins and transcription factor Sp1 in p21Wafl/Cip1 regulation by transforming growth factor-β
    • K. Pardali, A. Kurisaki, A. Morén, P. ten Dijke, D. Kardassis, A. Moustakas, Role of Smad proteins and transcription factor Sp1 in p21Wafl/Cip1 regulation by transforming growth factor-β. J. Biol. Chem. 275, 29244-29256 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 29244-29256
    • Pardali, K.1    Kurisaki, A.2    Morén, A.3    Ten Dijke, P.4    Kardassis, D.5    Moustakas, A.6
  • 22
    • 0028168242 scopus 로고
    • p15INK4B is a potential effector of TGF-β-induced cell-cycle arrest
    • G. J. Hannon, D. Beach, p15INK4B is a potential effector of TGF-β-induced cell-cycle arrest. Nature 371, 257-261 (1994).
    • (1994) Nature , vol.371 , pp. 257-261
    • Hannon, G.J.1    Beach, D.2
  • 23
    • 0033104505 scopus 로고    scopus 로고
    • TGF-β induces fibronectin synthesis through a c-Jun N-terminal kinase-dependent, Smad4-independent pathway
    • B. A. Hocevar, T. L. Brown, P. H. Howe, TGF-β induces fibronectin synthesis through a c-Jun N-terminal kinase-dependent, Smad4-independent pathway. EMBO J. 18, 1345-1356 (1999).
    • (1999) EMBO J. , vol.18 , pp. 1345-1356
    • Hocevar, B.A.1    Brown, T.L.2    Howe, P.H.3
  • 24
    • 0032101178 scopus 로고    scopus 로고
    • Direct binding of Smad3 and Smad4 to critical TGFβ-inducible elements in the promoter of human plasminogen activator inhibitor-type 1 gene
    • S. Dennler, S. Itoh, D. Vivien, P. ten Dijke, S. Huet, J. M. Gauthier, Direct binding of Smad3 and Smad4 to critical TGFβ-inducible elements in the promoter of human plasminogen activator inhibitor-type 1 gene. EMBO J. 17, 3091-3100 (1998).
    • (1998) EMBO J. , vol.17 , pp. 3091-3100
    • Dennler, S.1    Itoh, S.2    Vivien, D.3    Ten Dijke, P.4    Huet, S.5    Gauthier, J.M.6
  • 25
    • 0023654923 scopus 로고
    • Regulation of fibronectin and type I collagen mRNA levels by transforming growth factor-β
    • R. A. Ignotz, T. Endo, J. Massagué, Regulation of fibronectin and type I collagen mRNA levels by transforming growth factor-β. J. Biol. Chem. 262, 6443-6446 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 6443-6446
    • Ignotz, R.A.1    Endo, T.2    Massagué, J.3
  • 26
    • 58149213801 scopus 로고    scopus 로고
    • Non-Smad pathways in TGF-β signaling
    • Y. E. Zhang, Non-Smad pathways in TGF-β signaling. Cell Res. 19, 128-139 (2009).
    • (2009) Cell Res. , vol.19 , pp. 128-139
    • Zhang, Y.E.1
  • 28
    • 77957892223 scopus 로고    scopus 로고
    • Proteomics of Smad4 regulated transforming growth factor-β signalling in colon cancer cells
    • N. A. Ali, M. J. McKay, M. P. Molloy, Proteomics of Smad4 regulated transforming growth factor-β signalling in colon cancer cells. Mol. Biosyst. 6, 2332-2338 (2010).
    • (2010) Mol. Biosyst. , vol.6 , pp. 2332-2338
    • Ali, N.A.1    McKay, M.J.2    Molloy, M.P.3
  • 30
    • 79960815170 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics of transforming growth factor-β signaling in colon cancer cells
    • N. A. Ali, M. P. Molloy, Quantitative phosphoproteomics of transforming growth factor-β signaling in colon cancer cells. Proteomics 11, 3390-3401 (2011).
    • (2011) Proteomics , vol.11 , pp. 3390-3401
    • Ali, N.A.1    Molloy, M.P.2
  • 31
    • 26244454581 scopus 로고    scopus 로고
    • Phosphoproteome profiling of transforming growth factor (TGF)-β signaling: Abrogation of TGFβ1-dependent phosphorylation of transcription factor-II-I (TFII-I) enhances cooperation of TFII-I and Smad3 in transcription
    • T. Stasyk, A. Dubrovska, M. Lomnytska, I. Yakymovych, C. Wernstedt, C. H. Heldin, U. Hellman, S. Souchelnytskyi, Phosphoproteome profiling of transforming growth factor (TGF)-β signaling: Abrogation of TGFβ1-dependent phosphorylation of transcription factor-II-I (TFII-I) enhances cooperation of TFII-I and Smad3 in transcription. Mol. Biol. Cell 16, 4765-4780 (2005).
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4765-4780
    • Stasyk, T.1    Dubrovska, A.2    Lomnytska, M.3    Yakymovych, I.4    Wernstedt, C.5    Heldin, C.H.6    Hellman, U.7    Souchelnytskyi, S.8
  • 32
    • 0029070821 scopus 로고
    • A human keratinocyte cell line produces two autocrine growth inhibitors, transforming growth factor-β and insulin-like growth factor binding protein-6, in a calcium-and cell density-dependent manner
    • M. Kato, A. Ishizaki, U. Hellman, C.Wernstedt, M. Kyogoku, K. Miyazono, C. H. Heldin, K. Funa, A human keratinocyte cell line produces two autocrine growth inhibitors, transforming growth factor-β and insulin-like growth factor binding protein-6, in a calcium-and cell density-dependent manner. J. Biol. Chem. 270, 12373-12379 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 12373-12379
    • Kato, M.1    Ishizaki, A.2    Hellman, U.3    Wernstedt, C.4    Kyogoku, M.5    Miyazono, K.6    Heldin, C.H.7    Funa, K.8
  • 33
    • 0033720486 scopus 로고    scopus 로고
    • Up-modulation of the expression of functional keratinocyte growth factor receptors induced by high cell density in the human keratinocyte HaCaT cell line
    • A. Capone, V. Visco, F. Belleudi, C. Marchese, G. Cardinali, M. Bellocci, M. Picardo, L. Frati, M. R. Torrisi, Up-modulation of the expression of functional keratinocyte growth factor receptors induced by high cell density in the human keratinocyte HaCaT cell line. Cell Growth Differ. 11, 607-614 (2000).
    • (2000) Cell Growth Differ. , vol.11 , pp. 607-614
    • Capone, A.1    Visco, V.2    Belleudi, F.3    Marchese, C.4    Cardinali, G.5    Bellocci, M.6    Picardo, M.7    Frati, L.8    Torrisi, M.R.9
  • 34
    • 84907197082 scopus 로고    scopus 로고
    • MaxLFQ allows accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction
    • mcp.M113.031591
    • J. Cox, M. Y. Hein, C. A. Luber, I. Paron, N. Nagaraj, M. Mann, MaxLFQ allows accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction. Mol. Cell. Proteomics mcp.M113.031591 (2014).
    • (2014) Mol. Cell. Proteomics
    • Cox, J.1    Hein, M.Y.2    Luber, C.A.3    Paron, I.4    Nagaraj, N.5    Mann, M.6
  • 35
    • 0029073142 scopus 로고
    • Transforming growth factor β induces the cyclin-dependent kinase inhibitor p21 through a p53-independent mechanism
    • M. B. Datto, Y. Li, J. F. Panus, D. J. Howe, Y. Xiong, X. F. Wang, Transforming growth factor β induces the cyclin-dependent kinase inhibitor p21 through a p53-independent mechanism. Proc. Natl. Acad. Sci. U.S.A. 92, 5545-5549 (1995).
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5545-5549
    • Datto, M.B.1    Li, Y.2    Panus, J.F.3    Howe, D.J.4    Xiong, Y.5    Wang, X.F.6
  • 36
    • 27244443082 scopus 로고    scopus 로고
    • Proliferation marker Ki-67 in early breast cancer
    • A. Urruticoechea, I. E. Smith, M. Dowsett, Proliferation marker Ki-67 in early breast cancer. J. Clin. Oncol. 23, 7212-7220 (2005).
    • (2005) J. Clin. Oncol. , vol.23 , pp. 7212-7220
    • Urruticoechea, A.1    Smith, I.E.2    Dowsett, M.3
  • 37
    • 0028071664 scopus 로고
    • Cell cycle-dependent inhibition of p34cdc2 synthesis by transforming growth factor β1 in cycling epithelial cells
    • S. T. Eblen, M. P. Fautsch, R. J. Burnette, P. Joshi, E. B. Leof, Cell cycle-dependent inhibition of p34cdc2 synthesis by transforming growth factor β1 in cycling epithelial cells. Cell Growth Differ. 5, 109-116 (1994).
    • (1994) Cell Growth Differ. , vol.5 , pp. 109-116
    • Eblen, S.T.1    Fautsch, M.P.2    Burnette, R.J.3    Joshi, P.4    Leof, E.B.5
  • 38
    • 0032812933 scopus 로고    scopus 로고
    • Growth state-dependent regulation of plasminogen activator inhibitor type-1 gene expression during epithelial cell stimulation by serum and transforming growth factor-β1
    • J. R. Boehm, S. M. Kutz, E. H. Sage, L. Staiano-Coico, P. J. Higgins, Growth state-dependent regulation of plasminogen activator inhibitor type-1 gene expression during epithelial cell stimulation by serum and transforming growth factor-β1. J. Cell. Physiol. 181, 96-106 (1999).
    • (1999) J. Cell. Physiol. , vol.181 , pp. 96-106
    • Boehm, J.R.1    Kutz, S.M.2    Sage, E.H.3    Staiano-Coico, L.4    Higgins, P.J.5
  • 39
    • 75949103899 scopus 로고    scopus 로고
    • Integrin -TGF-β crosstalk in fibrosis, cancer and wound healing
    • C. Margadant, A. Sonnenberg, Integrin -TGF-β crosstalk in fibrosis, cancer and wound healing. EMBO Rep. 11, 97-105 (2010).
    • (2010) EMBO Rep. , vol.11 , pp. 97-105
    • Margadant, C.1    Sonnenberg, A.2
  • 40
    • 38149019302 scopus 로고    scopus 로고
    • Genome-wide impact of the BRG1 SWI/SNF chromatin remodeler on the transforming growth factor β transcriptional program
    • Q. R. Xi, W. He, X. H. F. Zhang, H. V. Le, J. Massagué, Genome-wide impact of the BRG1 SWI/SNF chromatin remodeler on the transforming growth factor β transcriptional program. J. Biol. Chem. 283, 1146-1155 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 1146-1155
    • Xi, Q.R.1    He, W.2    Zhang, X.H.F.3    Le, H.V.4    Massagué, J.5
  • 42
    • 23844543808 scopus 로고    scopus 로고
    • TAF4 inactivation in embryonic fibroblasts activates TGFβ signalling and autocrine growth
    • G. Mengus, A. Fadloun, D. Kobi, C. Thibault, L. Perletti, I. Michel, I. Davidson, TAF4 inactivation in embryonic fibroblasts activates TGFβ signalling and autocrine growth. EMBO J. 24, 2753-2767 (2005).
    • (2005) EMBO J. , vol.24 , pp. 2753-2767
    • Mengus, G.1    Fadloun, A.2    Kobi, D.3    Thibault, C.4    Perletti, L.5    Michel, I.6    Davidson, I.7
  • 44
    • 84894593599 scopus 로고    scopus 로고
    • Molecular mechanisms of epithelial-mesenchymal transition
    • S. Lamouille, J. Xu, R. Derynck, Molecular mechanisms of epithelial-mesenchymal transition. Nat. Rev. Mol. Cell Biol. 15, 178-196 (2014).
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 178-196
    • Lamouille, S.1    Xu, J.2    Derynck, R.3
  • 46
    • 84861968669 scopus 로고    scopus 로고
    • TGF-β-dependent active demethylation and expression of the p15ink4b tumor suppressor are impaired by the ZNF217/CoREST complex
    • G. Thillainadesan, J. M. Chitilian, M. Isovic, J. N. G. Ablack, J. S. Mymryk, M. Tini, J. Torchia, TGF-β-dependent active demethylation and expression of the p15ink4b tumor suppressor are impaired by the ZNF217/CoREST complex. Mol. Cell 46, 636-649 (2012).
    • (2012) Mol. Cell , vol.46 , pp. 636-649
    • Thillainadesan, G.1    Chitilian, J.M.2    Isovic, M.3    Ablack, J.N.G.4    Mymryk, J.S.5    Tini, M.6    Torchia, J.7
  • 47
    • 84873508256 scopus 로고    scopus 로고
    • 1D and 2D annotation enrichment: A statistical method integrating quantitative proteomics with complementary high-throughput data
    • J. Cox, M. Mann, 1D and 2D annotation enrichment: A statistical method integrating quantitative proteomics with complementary high-throughput data. BMC Bioinformatics 13 (Suppl. 16), S12 (2012).
    • (2012) BMC Bioinformatics , vol.13 , pp. S12
    • Cox, J.1    Mann, M.2
  • 48
    • 84874251061 scopus 로고    scopus 로고
    • PRSS23 is essential for the Snail-dependent endothelial-to-mesenchymal transition during valvulogenesis in zebrafish
    • I. H. Chen, H. H. Wang, Y. S. Hsieh, W. C. Huang, H. I. Yeh, Y. J. Chuang, PRSS23 is essential for the Snail-dependent endothelial-to-mesenchymal transition during valvulogenesis in zebrafish. Cardiovasc. Res. 97, 443-453 (2013).
    • (2013) Cardiovasc. Res. , vol.97 , pp. 443-453
    • Chen, I.H.1    Wang, H.H.2    Hsieh, Y.S.3    Huang, W.C.4    Yeh, H.I.5    Chuang, Y.J.6
  • 49
    • 84856255286 scopus 로고    scopus 로고
    • TGF-β1→SMAD/p53/ USF2→PAI-1 transcriptional axis in ureteral obstruction-induced renal fibrosis
    • R. Samarakoon, J. M. Overstreet, S. P. Higgins, P. J. Higgins, TGF-β1→SMAD/p53/ USF2→PAI-1 transcriptional axis in ureteral obstruction-induced renal fibrosis. Cell Tissue Res. 347, 117-128 (2012).
    • (2012) Cell Tissue Res. , vol.347 , pp. 117-128
    • Samarakoon, R.1    Overstreet, J.M.2    Higgins, S.P.3    Higgins, P.J.4
  • 51
    • 84864228827 scopus 로고    scopus 로고
    • The T box transcription factor TBX2 promotes epithelial-mesenchymal transition and invasion of normal and malignant breast epithelial cells
    • B. Wang, L. E. Lindley, V. Fernandez-Vega, M. E. Rieger, A. H. Sims, K. J. Briegel, The T box transcription factor TBX2 promotes epithelial-mesenchymal transition and invasion of normal and malignant breast epithelial cells. PLOS One 7, e41355 (2012).
    • (2012) PLOS One , vol.7 , pp. e41355
    • Wang, B.1    Lindley, L.E.2    Fernandez-Vega, V.3    Rieger, M.E.4    Sims, A.H.5    Briegel, K.J.6
  • 53
    • 0034596993 scopus 로고    scopus 로고
    • Smad2, Smad3 and Smad4 cooperate with Sp1 to induce p15Ink4B transcription in response to TGF- b
    • X. H. Feng, X. Lin, R. Derynck, Smad2, Smad3 and Smad4 cooperate with Sp1 to induce p15Ink4B transcription in response to TGF- b. EMBO J. 19, 5178-5193 (2000).
    • (2000) EMBO J. , vol.19 , pp. 5178-5193
    • Feng, X.H.1    Lin, X.2    Derynck, R.3
  • 54
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • S. E. Ong, B. Blagoev, I. Kratchmarova, D. B. Kristensen, H. Steen, A. Pandey, M. Mann, 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    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 55
    • 77952023070 scopus 로고    scopus 로고
    • Quantitative analysis of kinase-proximal signaling in lipopolysaccharide-induced innate immune response
    • K. Sharma, C. Kumar, G. Kéri, S. B. Breitkopf, F. S. Oppermann, H. Daub, Quantitative analysis of kinase-proximal signaling in lipopolysaccharide-induced innate immune response. J. Proteome Res. 9, 2539-2549 (2010).
    • (2010) J. Proteome Res. , vol.9 , pp. 2539-2549
    • Sharma, K.1    Kumar, C.2    Kéri, G.3    Breitkopf, S.B.4    Oppermann, F.S.5    Daub, H.6
  • 56
    • 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
    • P. V. Hornbeck, J. M. Kornhauser, S. Tkachev, B. Zhang, E. Skrzypek, B. Murray, V. Latham, M. Sullivan, PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 40, D261-D270 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. D261-D270
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5    Murray, B.6    Latham, V.7    Sullivan, M.8
  • 57
    • 0030613249 scopus 로고    scopus 로고
    • TbRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling
    • S. Abdollah, M. Macias-Silva, T. Tsukazaki, H. Hayashi, L. Attisano, J. L. Wrana, TbRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling. J. Biol. Chem. 272, 27678-27685 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 27678-27685
    • Abdollah, S.1    Macias-Silva, M.2    Tsukazaki, T.3    Hayashi, H.4    Attisano, L.5    Wrana, J.L.6
  • 58
    • 0030613262 scopus 로고    scopus 로고
    • Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-β signaling
    • S. Souchelnytskyi, K. Tamaki, U. Engstrom, C. Wernstedt, P. ten Dijke, C. H. Heldin, Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-β signaling. J. Biol. Chem. 272, 28107-28115 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 28107-28115
    • Souchelnytskyi, S.1    Tamaki, K.2    Engstrom, U.3    Wernstedt, C.4    Ten Dijke, P.5    Heldin, C.H.6
  • 59
    • 0345425059 scopus 로고    scopus 로고
    • Cdc2 and Cdk2 kinase activated by transforming growth factor-β 1 trigger apoptosis through the phosphorylation of retinoblastoma protein in FaO hepatoma cells
    • K. S. Choi, Y. W. Eom, Y. Kang, M. J. Ha, H. Rhee, J. W. Yoon, S. J. Kim, Cdc2 and Cdk2 kinase activated by transforming growth factor-β 1 trigger apoptosis through the phosphorylation of retinoblastoma protein in FaO hepatoma cells. J. Biol. Chem. 274, 31775-31783 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 31775-31783
    • Choi, K.S.1    Eom, Y.W.2    Kang, Y.3    Ha, M.J.4    Rhee, H.5    Yoon, J.W.6    Kim, S.J.7
  • 60
    • 84875513121 scopus 로고    scopus 로고
    • TGFβ-induced PI 3 kinase-dependent Mnk-1 activation is necessary for Ser-209 phosphorylation of eIF4E and mesangial cell hypertrophy
    • F. Das, N. Ghosh-Choudhury, A. Bera, B. S. Kasinath, G. G. Choudhury, TGFβ-induced PI 3 kinase-dependent Mnk-1 activation is necessary for Ser-209 phosphorylation of eIF4E and mesangial cell hypertrophy. J. Cell. Physiol. 228, 1617-1626 (2013).
    • (2013) J. Cell. Physiol. , vol.228 , pp. 1617-1626
    • Das, F.1    Ghosh-Choudhury, N.2    Bera, A.3    Kasinath, B.S.4    Choudhury, G.G.5
  • 61
    • 0242721599 scopus 로고    scopus 로고
    • Cell-type-specific activation of PAK2 by transforming growth factor β independent of Smad2 and Smad3
    • M. C. Wilkes, S. J. Murphy, N. Garamszegi, E. B. Leof, Cell-type-specific activation of PAK2 by transforming growth factor β independent of Smad2 and Smad3. Mol. Cell. Biol. 23, 8878-8889 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8878-8889
    • Wilkes, M.C.1    Murphy, S.J.2    Garamszegi, N.3    Leof, E.B.4
  • 62
    • 84883410452 scopus 로고    scopus 로고
    • TGFb receptor I transactivation mediates stretch-induced Pak1 activation and CTGF upregulation in mesangial cells
    • G. Chen, X. Chen, A. Sukumar, B. Gao, J. Curley, H. W. Schnaper, A. J. Ingram, J. C. Krepinsky, TGFb receptor I transactivation mediates stretch-induced Pak1 activation and CTGF upregulation in mesangial cells. J. Cell Sci. 126, 3697-3712 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 3697-3712
    • Chen, G.1    Chen, X.2    Sukumar, A.3    Gao, B.4    Curley, J.5    Schnaper, H.W.6    Ingram, A.J.7    Krepinsky, J.C.8
  • 63
    • 84861448736 scopus 로고    scopus 로고
    • TGF-β-induced activation of mTOR complex 2 drives epithelial-mesenchymal transition and cell invasion
    • S. Lamouille, E. Connolly, J. W. Smyth, R. J. Akhurst, R. Derynck, TGF-β-induced activation of mTOR complex 2 drives epithelial-mesenchymal transition and cell invasion. J. Cell Sci. 125, 1259-1273 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 1259-1273
    • Lamouille, S.1    Connolly, E.2    Smyth, J.W.3    Akhurst, R.J.4    Derynck, R.5
  • 64
    • 34547587877 scopus 로고    scopus 로고
    • Cell size and invasion in TGF-β-induced epithelial to mesenchymal transition is regulated by activation of the mTOR pathway
    • S. Lamouille, R. Derynck, Cell size and invasion in TGF-β-induced epithelial to mesenchymal transition is regulated by activation of the mTOR pathway. J. Cell Biol. 178, 437-451 (2007).
    • (2007) J. Cell Biol. , vol.178 , pp. 437-451
    • Lamouille, S.1    Derynck, R.2
  • 65
    • 0028009849 scopus 로고
    • The cell cycle and the retinoblastoma protein family
    • M. E. Ewen, The cell cycle and the retinoblastoma protein family. Cancer Metastasis Rev. 13, 45-66 (1994).
    • (1994) Cancer Metastasis Rev. , vol.13 , pp. 45-66
    • Ewen, M.E.1
  • 67
    • 84855658379 scopus 로고    scopus 로고
    • Human Protein Reference Database and Human Proteinpedia as resources for phosphoproteome analysis
    • R. Goel, H. C. Harsha, A. Pandey, T. S. Prasad, Human Protein Reference Database and Human Proteinpedia as resources for phosphoproteome analysis. Mol. Biosyst. 8, 453-463 (2012).
    • (2012) Mol. Biosyst. , vol.8 , pp. 453-463
    • Goel, R.1    Harsha, H.C.2    Pandey, A.3    Prasad, T.S.4
  • 68
    • 65549146320 scopus 로고    scopus 로고
    • Control of transforming growth factor b signal transduction by small GTPases
    • D. Kardassis, C. Murphy, T. Fotsis, A. Moustakas, C. Stournaras, Control of transforming growth factor b signal transduction by small GTPases. FEBS J. 276, 2947-2965 (2009).
    • (2009) FEBS J. , vol.276 , pp. 2947-2965
    • Kardassis, D.1    Murphy, C.2    Fotsis, T.3    Moustakas, A.4    Stournaras, C.5
  • 69
    • 84871948755 scopus 로고    scopus 로고
    • TGF-β signaling and epithelial-mesenchymal transition in cancer progression
    • Y. Katsuno, S. Lamouille, R. Derynck, TGF-β signaling and epithelial-mesenchymal transition in cancer progression. Curr. Opin. Oncol. 25, 76-84 (2013).
    • (2013) Curr. Opin. Oncol. , vol.25 , pp. 76-84
    • Katsuno, Y.1    Lamouille, S.2    Derynck, R.3
  • 71
    • 0026027660 scopus 로고
    • Differential phosphorylation of vertebrate p34cdc2 kinase at the G1/S and G2/M transitions of the cell-cycle - Identification of major phosphorylation sites
    • W. Krek, E. A. Nigg, Differential phosphorylation of vertebrate p34cdc2 kinase at the G1/S and G2/M transitions of the cell-cycle - Identification of major phosphorylation sites. EMBO J. 10, 305-316 (1991).
    • (1991) EMBO J. , vol.10 , pp. 305-316
    • Krek, W.1    Nigg, E.A.2
  • 72
    • 39449106065 scopus 로고    scopus 로고
    • Phosphorylation of Skp2 regulated by CDK2 and Cdc14B protects it from degradation by APCCdh1 in G1 phase
    • G. Rodier, P. Coulombe, P. L. Tanguay, C. Boutonnet, S. Meloche, Phosphorylation of Skp2 regulated by CDK2 and Cdc14B protects it from degradation by APCCdh1 in G1 phase. EMBO J. 27, 679-691 (2008).
    • (2008) EMBO J. , vol.27 , pp. 679-691
    • Rodier, G.1    Coulombe, P.2    Tanguay, P.L.3    Boutonnet, C.4    Meloche, S.5
  • 73
    • 0037178801 scopus 로고    scopus 로고
    • Distinct phosphorylation events regulate p130- and p107-mediated repression of E2F-4
    • T. Farkas, K. Hansen, K. Holm, J. Lukas, J. Bartek, Distinct phosphorylation events regulate p130- and p107-mediated repression of E2F-4. J. Biol. Chem. 277, 26741-26752 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 26741-26752
    • Farkas, T.1    Hansen, K.2    Holm, K.3    Lukas, J.4    Bartek, J.5
  • 74
    • 0038418869 scopus 로고    scopus 로고
    • Chk1 and Chk2 kinases in checkpoint control and cancer
    • J. Bartek, J. Lukas, Chk1 and Chk2 kinases in checkpoint control and cancer. Cancer Cell 3, 421-429 (2003).
    • (2003) Cancer Cell , vol.3 , pp. 421-429
    • Bartek, J.1    Lukas, J.2
  • 75
    • 35649021338 scopus 로고    scopus 로고
    • Stability of checkpoint kinase 2 is regulated via phosphorylation at serine 456
    • E. M. Kass, J. Ahn, T. Tanaka, W. A. Freed-Pastor, S. Keezer, C. Prives, Stability of checkpoint kinase 2 is regulated via phosphorylation at serine 456. J. Biol. Chem. 282, 30311-30321 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 30311-30321
    • Kass, E.M.1    Ahn, J.2    Tanaka, T.3    Freed-Pastor, W.A.4    Keezer, S.5    Prives, C.6
  • 78
    • 52049111663 scopus 로고    scopus 로고
    • TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-β
    • M. Yamashita, K. Fatyol, C. Y. Jin, X. C. Wang, Z. G. Liu, Y. E. Zhang, TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-β. Mol. Cell 31, 918-924 (2008).
    • (2008) Mol. Cell , vol.31 , pp. 918-924
    • Yamashita, M.1    Fatyol, K.2    Jin, C.Y.3    Wang, X.C.4    Liu, Z.G.5    Zhang, Y.E.6
  • 80
    • 24944497786 scopus 로고    scopus 로고
    • Non-Smad TGF-β signals
    • A. Moustakas, C. H. Heldin, Non-Smad TGF-β signals. J. Cell Sci. 118, 3573-3584 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 3573-3584
    • Moustakas, A.1    Heldin, C.H.2
  • 82
    • 0041816053 scopus 로고    scopus 로고
    • p130Cas couples the tyrosine kinase Bmx/Etk with regulation of the actin cytoskeleton and cell migration
    • Y. A. Abassi, M. Rehn, N. Ekman, K. Alitalo, K. Vuori, p130Cas couples the tyrosine kinase Bmx/Etk with regulation of the actin cytoskeleton and cell migration. J. Biol. Chem. 278, 35636-35643 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 35636-35643
    • Abassi, Y.A.1    Rehn, M.2    Ekman, N.3    Alitalo, K.4    Vuori, K.5
  • 84
    • 16844367763 scopus 로고    scopus 로고
    • The NF2 tumor suppressor Merlin and the ERM proteins interact with N-WASP and regulate its actin polymerization function
    • N. Manchanda, A. Lyubimova, H. Y. Ho, M. F. James, J. F. Gusella, N. Ramesh, S. B. Snapper, V. Ramesh, The NF2 tumor suppressor Merlin and the ERM proteins interact with N-WASP and regulate its actin polymerization function. J. Biol. Chem. 280, 12517-12522 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 12517-12522
    • Manchanda, N.1    Lyubimova, A.2    Ho, H.Y.3    James, M.F.4    Gusella, J.F.5    Ramesh, N.6    Snapper, S.B.7    Ramesh, V.8
  • 85
    • 34648819675 scopus 로고    scopus 로고
    • A C-terminal dimerization motif is required for focal adhesion targeting of Talin1 and the interaction of the Talin1 I/LWEQ module with F-actin
    • S. J. Smith, R. O. McCann, A C-terminal dimerization motif is required for focal adhesion targeting of Talin1 and the interaction of the Talin1 I/LWEQ module with F-actin. Biochemistry 46, 10886-10898 (2007).
    • (2007) Biochemistry , vol.46 , pp. 10886-10898
    • Smith, S.J.1    McCann, R.O.2
  • 86
    • 56649088324 scopus 로고    scopus 로고
    • A review of actin binding proteins: New perspectives
    • R. Uribe, D. Jay, A review of actin binding proteins: New perspectives. Mol. Biol. Rep. 36, 121-125 (2009).
    • (2009) Mol. Biol. Rep. , vol.36 , pp. 121-125
    • Uribe, R.1    Jay, D.2
  • 87
    • 33644534795 scopus 로고    scopus 로고
    • The tumor suppressor Smad4 is required for transforming growth factor β-induced epithelial to mesenchymal transition and bone metastasis of breast cancer cells
    • M. Deckers, M. van Dinther, J. Buijs, N. Que, C. Lowik, G. van der Pluijm, P. ten Dijke, The tumor suppressor Smad4 is required for transforming growth factor β-induced epithelial to mesenchymal transition and bone metastasis of breast cancer cells. Cancer Res. 66, 2202-2209 (2006).
    • (2006) Cancer Res. , vol.66 , pp. 2202-2209
    • Deckers, M.1    Van Dinther, M.2    Buijs, J.3    Que, N.4    Lowik, C.5    Van Der Pluijm, G.6    Ten Dijke, P.7
  • 88
    • 27544433149 scopus 로고    scopus 로고
    • Vitamin D and skin cancer: A problem in gene regulation
    • D. D. Bickle, Y. Oda, Z. Xie, Vitamin D and skin cancer: A problem in gene regulation. J. Steroid Biochem. Mol. Biol. 97, 83-91 (2005).
    • (2005) J. Steroid Biochem. Mol. Biol. , vol.97 , pp. 83-91
    • Bickle, D.D.1    Oda, Y.2    Xie, Z.3
  • 89
    • 84867125728 scopus 로고    scopus 로고
    • Loss of vitamin D receptor in chronic kidney disease: A potential mechanism linking inflammation to epithelial-to-mesenchymal transition
    • M. Xiong, J. B. Gong, Y. H. Liu, R. Xiang, X. Y. Tan, Loss of vitamin D receptor in chronic kidney disease: A potential mechanism linking inflammation to epithelial-to-mesenchymal transition. Am. J. Physiol. Renal Physiol. 303, F1107-F1115 (2012).
    • (2012) Am. J. Physiol. Renal Physiol. , vol.303 , pp. F1107-F1115
    • Xiong, M.1    Gong, J.B.2    Liu, Y.H.3    Xiang, R.4    Tan, X.Y.5
  • 91
    • 0037598870 scopus 로고    scopus 로고
    • Distinct endocytic pathways regulate TGF-β receptor signalling and turnover
    • G. M. Di Guglielmo, C. Le Roy, A. F. Goodfellow, J. L. Wrana, Distinct endocytic pathways regulate TGF-β receptor signalling and turnover. Nat. Cell Biol. 5, 410-421 (2003).
    • (2003) Nat. Cell Biol. , vol.5 , pp. 410-421
    • Di Guglielmo, G.M.1    Le Roy, C.2    Goodfellow, A.F.3    Wrana, J.L.4
  • 92
    • 11144296871 scopus 로고    scopus 로고
    • Lysosomal targeting of E-cadherin: A unique mechanism for the down-regulation of cell-cell adhesion during epithelial to mesenchymal transitions
    • F. Palacios, J. S. Tushir, Y. Fujita, C. D' Souza-Schorey, Lysosomal targeting of E-cadherin: A unique mechanism for the down-regulation of cell-cell adhesion during epithelial to mesenchymal transitions. Mol. Cell. Biol. 25, 389-402 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 389-402
    • Palacios, F.1    Tushir, J.S.2    Fujita, Y.3    D'Souza-Schorey, C.4
  • 93
    • 33748466150 scopus 로고    scopus 로고
    • Endocytic recycling pathways: Emerging regulators of cell migration
    • M. C. Jones, P. T. Caswell, J. C. Norman, Endocytic recycling pathways: Emerging regulators of cell migration. Curr. Opin. Cell Biol. 18, 549-557 (2006).
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 549-557
    • Jones, M.C.1    Caswell, P.T.2    Norman, J.C.3
  • 95
    • 0030978315 scopus 로고    scopus 로고
    • Repression of the CDK activator Cdc25A and cell-cycle arrest by cytokine TGF-β in cells lacking the CDK inhibitor p15
    • A. Iavarone, J. Massagué, Repression of the CDK activator Cdc25A and cell-cycle arrest by cytokine TGF-β in cells lacking the CDK inhibitor p15. Nature 387, 417-422 (1997).
    • (1997) Nature , vol.387 , pp. 417-422
    • Iavarone, A.1    Massagué, J.2
  • 98
    • 0032933352 scopus 로고    scopus 로고
    • E2F and histone deacetylase mediate transforming growth factor β repression of cdc25A during keratinocyte cell cycle arrest
    • A. Iavarone, J. Massagué, E2F and histone deacetylase mediate transforming growth factor β repression of cdc25A during keratinocyte cell cycle arrest. Mol. Cell. Biol. 19, 916-922 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 916-922
    • Iavarone, A.1    Massagué, J.2
  • 99
    • 49749085186 scopus 로고    scopus 로고
    • Expression and localization of Ski determine cell type - specific TGFβ signaling effects on the cell cycle
    • C. Jacob, H. Grabner, S. Atanasoski, U. Suter, Expression and localization of Ski determine cell type - specific TGFβ signaling effects on the cell cycle. J. Cell Biol. 182 519-530 (2008).
    • (2008) J. Cell Biol. , vol.182 , pp. 519-530
    • Jacob, C.1    Grabner, H.2    Atanasoski, S.3    Suter, U.4
  • 100
    • 2942518250 scopus 로고    scopus 로고
    • Lost in translation: Dysregulation of cap-dependent translation and cancer
    • M. A. Bjornsti, P. J. Houghton, Lost in translation: Dysregulation of cap-dependent translation and cancer. Cancer Cell 5, 519-523 (2004).
    • (2004) Cancer Cell , vol.5 , pp. 519-523
    • Bjornsti, M.A.1    Houghton, P.J.2
  • 101
    • 33750351403 scopus 로고    scopus 로고
    • Signal transduction: Protein synthesis and oncogenesis meet again
    • N. Sonenberg, A. Pause, Signal transduction: Protein synthesis and oncogenesis meet again. Science 314, 428-429 (2006).
    • (2006) Science , vol.314 , pp. 428-429
    • Sonenberg, N.1    Pause, A.2
  • 102
    • 70450221920 scopus 로고    scopus 로고
    • 4E-BP1 is a target of Smad4 essential for TGFβ-mediated inhibition of cell proliferation
    • R. Azar, A. Alard, C. Susini, C. Bousquet, S. Pyronnet, 4E-BP1 is a target of Smad4 essential for TGFβ-mediated inhibition of cell proliferation. EMBO J. 28, 3514-3522 (2009).
    • (2009) EMBO J. , vol.28 , pp. 3514-3522
    • Azar, R.1    Alard, A.2    Susini, C.3    Bousquet, C.4    Pyronnet, S.5
  • 103
    • 33845262863 scopus 로고    scopus 로고
    • Role of the Akt/FoxO3a pathway in TGF-β1-mediated mesangial cell dysfunction: A novel mechanism related to diabetic kidney disease
    • M. Kato, H. Yuan, Z. G. Xu, L. Lanting, S. L. Li, M. Wang, M. C. Hu, M. A. Reddy, R. Natarajan, Role of the Akt/FoxO3a pathway in TGF-β1-mediated mesangial cell dysfunction: A novel mechanism related to diabetic kidney disease. J. Am. Soc. Nephrol. 17, 3325-3335 (2006).
    • (2006) J. Am. Soc. Nephrol. , vol.17 , pp. 3325-3335
    • Kato, M.1    Yuan, H.2    Xu, Z.G.3    Lanting, L.4    Li, S.L.5    Wang, M.6    Hu, M.C.7    Reddy, M.A.8    Natarajan, R.9
  • 104
    • 0035800662 scopus 로고    scopus 로고
    • p90-RSK and Akt may promote rapid phosphorylation/inactivation of glycogen synthase kinase 3 in chemoattractant-stimulated neutrophils
    • D. D. De Mesquita, Q. Zhan, L. Crossley, J. A. Badwey, p90-RSK and Akt may promote rapid phosphorylation/inactivation of glycogen synthase kinase 3 in chemoattractant-stimulated neutrophils. FEBS Lett. 502, 84-88 (2001).
    • (2001) FEBS Lett. , vol.502 , pp. 84-88
    • De Mesquita, D.D.1    Zhan, Q.2    Crossley, L.3    Badwey, J.A.4
  • 105
    • 0027515127 scopus 로고
    • Inactivation of glycogen-synthase kinase-3β by phosphorylation: New kinase connections in insulin and growth-factor signaling
    • C. Sutherland, I. A. Leighton, P. Cohen, Inactivation of glycogen-synthase kinase-3β by phosphorylation: New kinase connections in insulin and growth-factor signaling. Biochem. J. 296, 15-19 (1993).
    • (1993) Biochem. J. , vol.296 , pp. 15-19
    • Sutherland, C.1    Leighton, I.A.2    Cohen, P.3
  • 106
    • 74849138924 scopus 로고    scopus 로고
    • Regulation of protein stability by GSK3 mediated phosphorylation
    • C. Xu, N. G. Kim, B. M. Gumbiner, Regulation of protein stability by GSK3 mediated phosphorylation. Cell Cycle 8, 4032-4039 (2009).
    • (2009) Cell Cycle , vol.8 , pp. 4032-4039
    • Xu, C.1    Kim, N.G.2    Gumbiner, B.M.3
  • 107
    • 84857364721 scopus 로고    scopus 로고
    • A Rac1/PAK1 cascade controls β-catenin activation in colon cancer cells
    • G. Zhu, Y. Wang, B. Huang, J. Liang, Y. Ding, A. Xu, W. Wu, A Rac1/PAK1 cascade controls β-catenin activation in colon cancer cells. Oncogene 31, 1001-1012 (2012).
    • (2012) Oncogene , vol.31 , pp. 1001-1012
    • Zhu, G.1    Wang, Y.2    Huang, B.3    Liang, J.4    Ding, Y.5    Xu, A.6    Wu, W.7
  • 108
    • 0035196587 scopus 로고    scopus 로고
    • Transforming growth factor β enhances epithelial cell survival via Akt-dependent regulation of FKHRL1
    • I. Shin, A. V. Bakin, U. Rodeck, A. Brunet, C. L. Arteaga, Transforming growth factor β enhances epithelial cell survival via Akt-dependent regulation of FKHRL1. Mol. Biol. Cell 12, 3328-3339 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3328-3339
    • Shin, I.1    Bakin, A.V.2    Rodeck, U.3    Brunet, A.4    Arteaga, C.L.5
  • 109
    • 84873401531 scopus 로고    scopus 로고
    • Using guanidine-hydrochloride for fast and efficient protein digestion and single-step affinity-purification mass spectrometry
    • J. W. Poulsen, C. T. Madsen, C. Young, F. M. Poulsen, M. L. Nielsen, Using guanidine-hydrochloride for fast and efficient protein digestion and single-step affinity-purification mass spectrometry. J. Proteome Res. 12, 1020-1030 (2013).
    • (2013) J. Proteome Res. , vol.12 , pp. 1020-1030
    • Poulsen, J.W.1    Madsen, C.T.2    Young, C.3    Poulsen, F.M.4    Nielsen, M.L.5
  • 110
    • 84895538371 scopus 로고    scopus 로고
    • Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells
    • N. A. Kulak, G. Pichler, I. Paron, N. Nagaraj, M. Mann, Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells. Nat. Methods 11, 319-324 (2014).
    • (2014) Nat. Methods , vol.11 , pp. 319-324
    • Kulak, N.A.1    Pichler, G.2    Paron, I.3    Nagaraj, N.4    Mann, M.5
  • 111
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • J. V. Olsen, B. Blagoev, F. Gnad, B. Macek, C. Kumar, P. Mortensen, M. Mann, Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648 (2006).
    • (2006) Cell , vol.127 , 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
  • 112
    • 78649849874 scopus 로고    scopus 로고
    • Feasibility of large-scale phosphoproteomics with higher energy collisional dissociation fragmentation
    • N. Nagaraj, R. C. J. D'Souza, J. Cox, J. V. Olsen, M. Mann, Feasibility of large-scale phosphoproteomics with higher energy collisional dissociation fragmentation. J. Proteome Res. 9, 6786-6794 (2010).
    • (2010) J. Proteome Res. , vol.9 , pp. 6786-6794
    • Nagaraj, N.1    D'Souza, R.C.J.2    Cox, J.3    Olsen, J.V.4    Mann, M.5
  • 113
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • J. R. Wisniewski, A. Zougman, N. Nagaraj, M. Mann, Universal sample preparation method for proteome analysis. Nat. Methods 6, 359-362 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 115
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • J. Rappsilber, Y. Ishihama, M. Mann, 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).
    • (2003) Anal. Chem. , vol.75 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 117
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.P.B.- range mass accuracies and proteome-wide protein quantification
    • J. Cox, M. Mann, MaxQuant enables high peptide identification rates, individualized p.p.b.- range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372 (2008).
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 119
    • 79960976768 scopus 로고    scopus 로고
    • UniProt Knowledgebase: A hub of integrated protein data
    • M. Magrane, U. Consortium, UniProt Knowledgebase: A hub of integrated protein data. Database 2011, bar009 (2011).
    • (2011) Database , vol.2011 , pp. bar009
    • Magrane, M.1
  • 120
    • 84857938446 scopus 로고    scopus 로고
    • Comparative proteomic analysis of eleven common cell lines reveals ubiquitous but varying expression of most proteins
    • M111.014050
    • T. Geiger, A. Wehner, C. Schaab, J. Cox, M. Mann, 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
  • 121
    • 0035942271 scopus 로고    scopus 로고
    • Significance analysis of microarrays applied to the ionizing radiation response
    • V. G. Tusher, R. Tibshirani, G. Chu, Significance analysis of microarrays applied to the ionizing radiation response. Proc. Natl. Acad. Sci. U.S.A. 98, 5116-5121 (2001).
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 5116-5121
    • Tusher, V.G.1    Tibshirani, R.2    Chu, G.3
  • 125
    • 84894571860 scopus 로고    scopus 로고
    • Causal analysis approaches in Ingenuity Pathway Analysis
    • A. Krämer, J. Green, J. Pollard Jr., S. Tugendreich, Causal analysis approaches in Ingenuity Pathway Analysis. Bioinformatics 30, 523-530 (2014).
    • (2014) Bioinformatics , vol.30 , pp. 523-530
    • Krämer, A.1    Green, J.2    Pollard, J.3    Tugendreich, S.4


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