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Volumn 9, Issue 7, 2010, Pages 3465-3478

14-3-3 epsilon dynamically interacts with key components of mitogen-activated protein kinase signal module for selective modulation of the TNF-aα-Induced time course-dependent NF-κb activity

Author keywords

14 3 3 ; Amino acid coded mass tagging; immune response; LC MS MS; nuclear factor kappa B; PPM1B; TAK1; tumor necrosis factor R

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOPROTEIN PHOSPHATASE 2; PHOSPHOPROTEIN PHOSPHATASE 2C BETA; PROTEIN 14 3 3; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; CARRIER PROTEIN; DNA HELICASE; FLAG PEPTIDE; MAP KINASE KINASE KINASE 7; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; OLIGOPEPTIDE; PEPTIDE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN PHOSPHATASE 2C; RUVBL2 PROTEIN, HUMAN; YWHAE PROTEIN, HUMAN;

EID: 77954374360     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr9011377     Document Type: Article
Times cited : (48)

References (91)
  • 1
    • 0035444539 scopus 로고    scopus 로고
    • Signal transduction by tumor necrosis factor and its relatives
    • Baud, V.; Karin, M. Signal transduction by tumor necrosis factor and its relatives Trends Cell Biol. 2001, 11 (9) 372-377
    • (2001) Trends Cell Biol. , vol.11 , Issue.9 , pp. 372-377
    • Baud, V.1    Karin, M.2
  • 2
    • 0028244816 scopus 로고
    • Tumor-necrosis-factor - A pleiotropic cytokine and therapeutic target
    • Tracey, K. J.; Cerami, A. Tumor-necrosis-factor-a pleiotropic cytokine and therapeutic target Ann. Rev. Med. 1994, 45, 491-503
    • (1994) Ann. Rev. Med. , vol.45 , pp. 491-503
    • Tracey, K.J.1    Cerami, A.2
  • 3
    • 21244496344 scopus 로고    scopus 로고
    • NF-kB in development and progression of human cancer
    • Dolcet, X.; Llobet, D.; Pallares, J.; Matias-Guiu, X. NF-kB in development and progression of human cancer Virchows Arch. 2005, 446 (5) 475-82
    • (2005) Virchows Arch. , vol.446 , Issue.5 , pp. 475-482
    • Dolcet, X.1    Llobet, D.2    Pallares, J.3    Matias-Guiu, X.4
  • 4
    • 0035409876 scopus 로고    scopus 로고
    • Nf-kB transcription factor: Role in the pathogenesis of inflammatory, autoimmune, and neoplastic diseases and therapy implications
    • Giuliani, C.; Napolitano, G.; Bucci, I.; Montani, V.; Monaco, F. [Nf-kB transcription factor: role in the pathogenesis of inflammatory, autoimmune, and neoplastic diseases and therapy implications] La Clin. Ter. 2001, 152 (4) 249-53
    • (2001) La Clin. Ter. , vol.152 , Issue.4 , pp. 249-253
    • Giuliani, C.1    Napolitano, G.2    Bucci, I.3    Montani, V.4    Monaco, F.5
  • 5
    • 0034574498 scopus 로고    scopus 로고
    • The ubiquitin-dependent proteolytic system and other potential targets for the modulation of nuclear factor-kB (NF-kB)
    • Magnani, M.; Crinelli, R.; Bianchi, M.; Antonelli, A. The ubiquitin-dependent proteolytic system and other potential targets for the modulation of nuclear factor-kB (NF-kB) Curr. Drug Targets 2000, 1 (4) 387-99
    • (2000) Curr. Drug Targets , vol.1 , Issue.4 , pp. 387-399
    • Magnani, M.1    Crinelli, R.2    Bianchi, M.3    Antonelli, A.4
  • 6
    • 40949123149 scopus 로고    scopus 로고
    • Activation of innate immunity system during aging: NF-kappa B signaling is the molecular culprit of inflamm-aging
    • Salminen, A.; Huuskonen, J.; Ojala, J.; Kauppinen, A.; Kaarniranta, K.; Suuronen, T. Activation of innate immunity system during aging: NF-kappa B signaling is the molecular culprit of inflamm-aging Ageing Res. Rev. 2008, 7 (2) 83-105
    • (2008) Ageing Res. Rev. , vol.7 , Issue.2 , pp. 83-105
    • Salminen, A.1    Huuskonen, J.2    Ojala, J.3    Kauppinen, A.4    Kaarniranta, K.5    Suuronen, T.6
  • 9
    • 1342285692 scopus 로고    scopus 로고
    • Tumor necrosis factor: An apoptosis JuNKie
    • Varfolomeev, E. E.; Ashkenazi, A. Tumor necrosis factor: An apoptosis JuNKie Cell 2004, 116 (4) 491-497
    • (2004) Cell , vol.116 , Issue.4 , pp. 491-497
    • Varfolomeev, E.E.1    Ashkenazi, A.2
  • 13
    • 38049018539 scopus 로고    scopus 로고
    • 14-3-3 proteins recognize a histone code at histone H3 and are required for transcriptional activation
    • Winter, S.; Simboeck, E.; Fischle, W.; Zupkovitz, G.; Dohnal, I.; Mechtler, K.; Ammerer, G.; Seiser, C. 14-3-3 proteins recognize a histone code at histone H3 and are required for transcriptional activation EMBO J. 2008, 27 (1) 88-99
    • (2008) EMBO J. , vol.27 , Issue.1 , pp. 88-99
    • Winter, S.1    Simboeck, E.2    Fischle, W.3    Zupkovitz, G.4    Dohnal, I.5    Mechtler, K.6    Ammerer, G.7    Seiser, C.8
  • 14
    • 37749024291 scopus 로고    scopus 로고
    • 14-3-3 Cruciform-binding proteins as regulators of eukaryotic DNA replication
    • Zannis-Hadjopoulos, M.; Yahyaoui, W.; Callejo, M. 14-3-3 Cruciform-binding proteins as regulators of eukaryotic DNA replication Trends in Biochem. Sci. 2008, 33 (1) 44-50
    • (2008) Trends in Biochem. Sci. , vol.33 , Issue.1 , pp. 44-50
    • Zannis-Hadjopoulos, M.1    Yahyaoui, W.2    Callejo, M.3
  • 15
    • 33847296214 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae 14-3-3 proteins Bmh1 and Bmh2 directly influence the DNA damage-dependent functions of Rad53
    • Usui, T.; Petrini, J. H. The Saccharomyces cerevisiae 14-3-3 proteins Bmh1 and Bmh2 directly influence the DNA damage-dependent functions of Rad53 Proc. Natl. Acad. Sci. U. S. A. 2007, 104 (8) 2797-2802
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , Issue.8 , pp. 2797-2802
    • Usui, T.1    Petrini, J.H.2
  • 16
    • 33644858078 scopus 로고    scopus 로고
    • 14-3-3 proteins integrate E2F activity with the DNA damage response
    • Milton, A. H.; Khaire, N.; Ingram, L.; O'Donnell, A. J.; La Thangue, N. B. 14-3-3 proteins integrate E2F activity with the DNA damage response EMBO J. 2006, 25 (5) 1046-57
    • (2006) EMBO J. , vol.25 , Issue.5 , pp. 1046-1057
    • Milton, A.H.1    Khaire, N.2    Ingram, L.3    O'Donnell, A.J.4    La Thangue, N.B.5
  • 17
    • 39749151070 scopus 로고    scopus 로고
    • G(1) to S phase transition protein 1 induces apoptosis signal-regulating kinase 1 activation by dissociating 14-3-3 from ASK1
    • Lee, J. A.; Park, J. E.; Lee, D. H.; Park, S. G.; Myung, P. K.; Park, B. C.; Cho, S. G(1) to S phase transition protein 1 induces apoptosis signal-regulating kinase 1 activation by dissociating 14-3-3 from ASK1 Oncogene 2008, 27 (9) 1297-1305
    • (2008) Oncogene , vol.27 , Issue.9 , pp. 1297-1305
    • Lee, J.A.1    Park, J.E.2    Lee, D.H.3    Park, S.G.4    Myung, P.K.5    Park, B.C.6    Cho, S.7
  • 18
    • 33646903670 scopus 로고    scopus 로고
    • Dynamic 14-3-3/client protein interactions integrate survival and apoptotic pathways
    • Porter, G. W.; Khuri, F. R.; Fu, H. Dynamic 14-3-3/client protein interactions integrate survival and apoptotic pathways Semin. Cancer Biol. 2006, 16 (3) 193-202
    • (2006) Semin. Cancer Biol. , vol.16 , Issue.3 , pp. 193-202
    • Porter, G.W.1    Khuri, F.R.2    Fu, H.3
  • 19
    • 2342651419 scopus 로고    scopus 로고
    • 14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking
    • Rubio, M. P.; Geraghty, K. M.; Wong, B. H. C.; Wood, N. T.; Campbell, D. G.; Morrice, N.; Mackintosh, C. 14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking Biochem. J. 2004, 379, 395-408
    • (2004) Biochem. J. , vol.379 , pp. 395-408
    • Rubio, M.P.1    Geraghty, K.M.2    Wong, B.H.C.3    Wood, N.T.4    Campbell, D.G.5    Morrice, N.6    MacKintosh, C.7
  • 20
    • 3543035767 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins
    • Meek, S. E. M.; Lane, W. S.; Piwnica-Worms, H. Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins J. Biol. Chem. 2004, 279 (31) 32046-32054
    • (2004) J. Biol. Chem. , vol.279 , Issue.31 , pp. 32046-32054
    • Meek, S.E.M.1    Lane, W.S.2    Piwnica-Worms, H.3
  • 23
    • 33644778718 scopus 로고    scopus 로고
    • Rapid identification of 14-3-3-binding proteins by protein microarray analysis
    • Satoh, J.; Nanri, Y.; Yamamura, T. Rapid identification of 14-3-3-binding proteins by protein microarray analysis J. Neurosci. Methods 2006, 152 (1-2) 278-288
    • (2006) J. Neurosci. Methods , vol.152 , Issue.1-2 , pp. 278-288
    • Satoh, J.1    Nanri, Y.2    Yamamura, T.3
  • 24
    • 21044434194 scopus 로고    scopus 로고
    • Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
    • Benzinger, A.; Muster, N.; Koch, H. B.; Yates, J. R.; Hermeking, H. Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer Mol. Cell. Proteomics 2005, 4 (6) 785-795
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.6 , pp. 785-795
    • Benzinger, A.1    Muster, N.2    Koch, H.B.3    Yates, J.R.4    Hermeking, H.5
  • 26
    • 55149120989 scopus 로고    scopus 로고
    • Reduced expression of 14-3-3 gamma in uterine leiomyoma as identified by proteomics
    • Lv, J.; Zhu, X.; Dong, K.; Lin, Y.; Hu, Y.; Zhu, C., Reduced expression of 14-3-3 gamma in uterine leiomyoma as identified by proteomics. Fertil. Steril. 2008, 1892 - 1898.
    • (2008) Fertil. Steril. , pp. 1892-1898
    • Lv, J.1    Zhu, X.2    Dong, K.3    Lin, Y.4    Hu, Y.5    Zhu, C.6
  • 28
    • 34249791171 scopus 로고    scopus 로고
    • Increases in expression of 14-3-3 eta and 14-3-3 zeta transcripts during neuroprotection induced by delta9-tetrahydrocannabinol in AF5 cells
    • Chen, J.; Lee, C. T.; Errico, S. L.; Becker, K. G.; Freed, W. J. Increases in expression of 14-3-3 eta and 14-3-3 zeta transcripts during neuroprotection induced by delta9-tetrahydrocannabinol in AF5 cells J. Neurosci. Res. 2007, 85 (8) 1724-33
    • (2007) J. Neurosci. Res. , vol.85 , Issue.8 , pp. 1724-1733
    • Chen, J.1    Lee, C.T.2    Errico, S.L.3    Becker, K.G.4    Freed, W.J.5
  • 29
    • 34547955936 scopus 로고    scopus 로고
    • Detection of high levels of 2 specific isoforms of 14-3-3 proteins in synovial fluid from patients with joint inflammation
    • Kilani, R. T.; Maksymowych, W. P.; Aitken, A.; Boire, G.; St-Pierre, Y.; Li, Y.; Ghahary, A. Detection of high levels of 2 specific isoforms of 14-3-3 proteins in synovial fluid from patients with joint inflammation J. Rheumatol. 2007, 34 (8) 1650-7
    • (2007) J. Rheumatol. , vol.34 , Issue.8 , pp. 1650-1657
    • Kilani, R.T.1    Maksymowych, W.P.2    Aitken, A.3    Boire, G.4    St-Pierre, Y.5    Li, Y.6    Ghahary, A.7
  • 30
    • 0029815121 scopus 로고    scopus 로고
    • Molecular evolution of the 14-3-3 protein family
    • Wang, W.; Shakes, D. C. Molecular evolution of the 14-3-3 protein family J. Mol. Evol. 1996, 43 (4) 384-98
    • (1996) J. Mol. Evol. , vol.43 , Issue.4 , pp. 384-398
    • Wang, W.1    Shakes, D.C.2
  • 32
    • 34248174248 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs induce colorectal cancer cell apoptosis by suppressing 14-3-3epsilon
    • Liou, J. Y.; Ghelani, D.; Yeh, S.; Wu, K. K. Nonsteroidal anti-inflammatory drugs induce colorectal cancer cell apoptosis by suppressing 14-3-3epsilon Cancer Res. 2007, 67 (7) 3185-3191
    • (2007) Cancer Res. , vol.67 , Issue.7 , pp. 3185-3191
    • Liou, J.Y.1    Ghelani, D.2    Yeh, S.3    Wu, K.K.4
  • 33
    • 11144256205 scopus 로고    scopus 로고
    • Isoform-specific expression of 14-3-3 proteins in human lung cancer tissues
    • Qi, W.; Liu, X.; Qiao, D.; Martinez, J. D. Isoform-specific expression of 14-3-3 proteins in human lung cancer tissues Int. J. Cancer 2005, 113 (3) 359-363
    • (2005) Int. J. Cancer , vol.113 , Issue.3 , pp. 359-363
    • Qi, W.1    Liu, X.2    Qiao, D.3    Martinez, J.D.4
  • 34
    • 34447259106 scopus 로고    scopus 로고
    • Proteomic profiling of MCF-7 breast cancer cells with chemoresistance to different types of anti-cancer drugs
    • Chuthapisith, S.; Layfield, R.; Kerr, I. D.; Hughes, C.; Eremin, O. Proteomic profiling of MCF-7 breast cancer cells with chemoresistance to different types of anti-cancer drugs Int. J. Oncol. 2007, 30 (6) 1545-51
    • (2007) Int. J. Oncol. , vol.30 , Issue.6 , pp. 1545-1551
    • Chuthapisith, S.1    Layfield, R.2    Kerr, I.D.3    Hughes, C.4    Eremin, O.5
  • 35
    • 0000385424 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis map of the human hepatocellular carcinoma cell line, HCC-M, and identification of the separated proteins by mass spectrometry
    • Seow, T. K.; Ong, S. E.; Liang, R.; Ren, E. C.; Chan, L.; Ou, K.; Chung, M. C. M. Two-dimensional electrophoresis map of the human hepatocellular carcinoma cell line, HCC-M, and identification of the separated proteins by mass spectrometry Electrophoresis 2000, 21 (9) 1787-1813
    • (2000) Electrophoresis , vol.21 , Issue.9 , pp. 1787-1813
    • Seow, T.K.1    Ong, S.E.2    Liang, R.3    Ren, E.C.4    Chan, L.5    Ou, K.6    Chung, M.C.M.7
  • 36
    • 33845341103 scopus 로고    scopus 로고
    • Interaction of HCV core protein with 14-3-3 epsilon protein releases Bax to activate apoptosis
    • Lee, S. K.; Park, S. O.; Joe, C. O.; Kim, Y. S. Interaction of HCV core protein with 14-3-3 epsilon protein releases Bax to activate apoptosis Biochem. Biophys. Res. Commun. 2007, 352 (3) 756-762
    • (2007) Biochem. Biophys. Res. Commun. , vol.352 , Issue.3 , pp. 756-762
    • Lee, S.K.1    Park, S.O.2    Joe, C.O.3    Kim, Y.S.4
  • 37
    • 0029738794 scopus 로고    scopus 로고
    • 14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome region
    • Chong, S. S.; Tanigami, A.; Roschke, A. V.; Ledbetter, D. H. 14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome region Genome Res. 1996, 6 (8) 735-741
    • (1996) Genome Res. , vol.6 , Issue.8 , pp. 735-741
    • Chong, S.S.1    Tanigami, A.2    Roschke, A.V.3    Ledbetter, D.H.4
  • 38
    • 34248174248 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs induce colorectal cancer cell apoptosis by suppressing 14-3-3 epsilon
    • Liou, J. Y.; Ghelani, D.; Yeh, S.; Wu, K. K. Nonsteroidal anti-inflammatory drugs induce colorectal cancer cell apoptosis by suppressing 14-3-3 epsilon Cancer Res. 2007, 67 (7) 3185-3191
    • (2007) Cancer Res. , vol.67 , Issue.7 , pp. 3185-3191
    • Liou, J.Y.1    Ghelani, D.2    Yeh, S.3    Wu, K.K.4
  • 39
    • 20844447127 scopus 로고    scopus 로고
    • In vivo dual-tagging proteomic approach in studying signaling pathways in immune response
    • Wang, T. Y.; Gu, S.; Ronni, T.; Du, Y. C.; Chen, M. In vivo dual-tagging proteomic approach in studying signaling pathways in immune response J. Proteome Res. 2005, 4 (3) 941-949
    • (2005) J. Proteome Res. , vol.4 , Issue.3 , pp. 941-949
    • Wang, T.Y.1    Gu, S.2    Ronni, T.3    Du, Y.C.4    Chen, M.5
  • 40
    • 33745623633 scopus 로고    scopus 로고
    • The dynamic alterations of H2AX complex during DNA repair detected by a proteomic approach reveal the critical roles of Ca2+/calmodulin in the ionizing radiation-induced cell cycle arrest
    • Du, Y. C.; Gu, S.; Zhou, J. H.; Wang, T. Y.; Cai, H.; MacInnes, M. A.; Bradbury, E. M.; Chen, X. The dynamic alterations of H2AX complex during DNA repair detected by a proteomic approach reveal the critical roles of Ca2+/calmodulin in the ionizing radiation-induced cell cycle arrest Mol. Cell. Proteomics 2006, 5 (6) 1033-1044
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.6 , pp. 1033-1044
    • Du, Y.C.1    Gu, S.2    Zhou, J.H.3    Wang, T.Y.4    Cai, H.5    MacInnes, M.A.6    Bradbury, E.M.7    Chen, X.8
  • 41
    • 60449087924 scopus 로고    scopus 로고
    • Analysis of the protein complex associated with 14-3-3 epsilon by a deuterated-leucine labeling quantitative proteomics strategy
    • Liang, S.; Yu, Y.; Yang, P.; Gu, S.; Xue, Y.; Chen, X. Analysis of the protein complex associated with 14-3-3 epsilon by a deuterated-leucine labeling quantitative proteomics strategy J. Chromatogr., B 2009, 877 (7) 627-634
    • (2009) J. Chromatogr., B , vol.877 , Issue.7 , pp. 627-634
    • Liang, S.1    Yu, Y.2    Yang, P.3    Gu, S.4    Xue, Y.5    Chen, X.6
  • 42
    • 30744432140 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of the tumor necrosis factor pathway
    • Cantin, G. T.; Venable, J. D.; Cociorva, D.; Yates, J. R. Quantitative phosphoproteomic analysis of the tumor necrosis factor pathway J. Proteome Res. 2006, 5 (1) 127-134
    • (2006) J. Proteome Res. , vol.5 , Issue.1 , pp. 127-134
    • Cantin, G.T.1    Venable, J.D.2    Cociorva, D.3    Yates, J.R.4
  • 44
    • 0025730640 scopus 로고
    • A rapid micropreparation technique for extraction of DNA-binding proteins from limiting numbers of mammalian-cells
    • Andrews, N. C.; Faller, D. V. A rapid micropreparation technique for extraction of DNA-binding proteins from limiting numbers of mammalian-cells Nucleic Acids Res. 1991, 19 (9) 2499-2499
    • (1991) Nucleic Acids Res. , vol.19 , Issue.9 , pp. 2499-2499
    • Andrews, N.C.1    Faller, D.V.2
  • 45
    • 0030698062 scopus 로고    scopus 로고
    • 14-3-3 is phosphorylated by casein kinase i on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction
    • Dubois, T.; Rommel, C.; Howell, S.; Steinhussen, U.; Soneji, Y.; Morrice, N.; Moelling, K.; Aitken, A. 14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction J. Biol. Chem. 1997, 272 (46) 28882-28888
    • (1997) J. Biol. Chem. , vol.272 , Issue.46 , pp. 28882-28888
    • Dubois, T.1    Rommel, C.2    Howell, S.3    Steinhussen, U.4    Soneji, Y.5    Morrice, N.6    Moelling, K.7    Aitken, A.8
  • 47
    • 34248570795 scopus 로고    scopus 로고
    • Ubiquitin-mediated activation of TAK1 and IKK
    • Adhikari, A.; Xu, M.; Chen, Z. J. Ubiquitin-mediated activation of TAK1 and IKK Oncogene 2007, 26 (22) 3214-3226
    • (2007) Oncogene , vol.26 , Issue.22 , pp. 3214-3226
    • Adhikari, A.1    Xu, M.2    Chen, Z.J.3
  • 49
    • 0035423794 scopus 로고    scopus 로고
    • Mutations in the Drosophila dTAK1 gene reveal a conserved function or MAPKKKs in the control of rel/NF-kappa B-dependent innate immune responses
    • Vidal, S.; Khush, R. S.; Leulier, F.; Tzou, P.; Nakamura, M.; Lemaitre, B. Mutations in the Drosophila dTAK1 gene reveal a conserved function or MAPKKKs in the control of rel/NF-kappa B-dependent innate immune responses Genes Dev. 2001, 15 (15) 1900-1912
    • (2001) Genes Dev. , vol.15 , Issue.15 , pp. 1900-1912
    • Vidal, S.1    Khush, R.S.2    Leulier, F.3    Tzou, P.4    Nakamura, M.5    Lemaitre, B.6
  • 53
    • 2342629277 scopus 로고    scopus 로고
    • The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes
    • Sun, L. J.; Deng, L.; Ea, C. K.; Xia, Z. P.; Chen, Z. J. J. The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes Mol. Cell 2004, 14 (3) 289-301
    • (2004) Mol. Cell , vol.14 , Issue.3 , pp. 289-301
    • Sun, L.J.1    Deng, L.2    Ea, C.K.3    Xia, Z.P.4    Chen, Z.J.J.5
  • 55
    • 33745955405 scopus 로고    scopus 로고
    • PP2C family members play key roles in regulation of cell survival and apoptosis
    • Tamura, S.; Toriumi, S.; Saito, J.; Awano, K.; Kudo, T.; Kobayashi, T. PP2C family members play key roles in regulation of cell survival and apoptosis Cancer Sci. 2006, 97 (7) 563-567
    • (2006) Cancer Sci. , vol.97 , Issue.7 , pp. 563-567
    • Tamura, S.1    Toriumi, S.2    Saito, J.3    Awano, K.4    Kudo, T.5    Kobayashi, T.6
  • 56
    • 38149030719 scopus 로고    scopus 로고
    • Phosphatases, DNA damage checkpoints and checkpoint deactivation
    • Heideker, J.; Lis, E. T.; Romesberg, F. E. Phosphatases, DNA damage checkpoints and checkpoint deactivation Cell Cycle 2007, 6 (24) 3058-3064
    • (2007) Cell Cycle , vol.6 , Issue.24 , pp. 3058-3064
    • Heideker, J.1    Lis, E.T.2    Romesberg, F.E.3
  • 57
    • 34248670864 scopus 로고    scopus 로고
    • Protein phosphatases types 2Calpha and 2Cbeta in apoptosis
    • Klumpp, S.; Thissen, M. C.; Krieglstein, J. Protein phosphatases types 2Calpha and 2Cbeta in apoptosis Biochem. Soc. Trans. 2006, 34 (Pt 6) 1370-1375
    • (2006) Biochem. Soc. Trans. , vol.34 , Issue.PART 6 , pp. 1370-1375
    • Klumpp, S.1    Thissen, M.C.2    Krieglstein, J.3
  • 58
    • 2442602365 scopus 로고    scopus 로고
    • Plant PP2C phosphatases: Emerging functions in stress signaling
    • Schweighofer, A.; Hirt, H.; Meskiene, I. Plant PP2C phosphatases: emerging functions in stress signaling Trends Plant Sci. 2004, 9 (5) 236-243
    • (2004) Trends Plant Sci. , vol.9 , Issue.5 , pp. 236-243
    • Schweighofer, A.1    Hirt, H.2    Meskiene, I.3
  • 59
    • 34247489726 scopus 로고    scopus 로고
    • Inflammation in obesity is the common link between defects in fatty acid metabolism and insulin resistance
    • Steinberg, G. R. Inflammation in obesity is the common link between defects in fatty acid metabolism and insulin resistance Cell Cycle 2007, 6 (8) 888-894
    • (2007) Cell Cycle , vol.6 , Issue.8 , pp. 888-894
    • Steinberg, G.R.1
  • 60
    • 33745955405 scopus 로고    scopus 로고
    • PP2C family members play key roles in regulation of cell survival and apoptosis
    • Tamura, S.; Toriumi, S.; Saito, J.; Awano, K.; Kudo, T. A.; Kobayashi, T. PP2C family members play key roles in regulation of cell survival and apoptosis Cancer Sci. 2006, 97 (7) 563-7
    • (2006) Cancer Sci. , vol.97 , Issue.7 , pp. 563-567
    • Tamura, S.1    Toriumi, S.2    Saito, J.3    Awano, K.4    Kudo, T.A.5    Kobayashi, T.6
  • 61
    • 0345826130 scopus 로고    scopus 로고
    • Protein phosphatase 2C beta association with the i kappa B kinase complex is involved in regulating NF-kappa B activity
    • Prajapati, S.; Verma, U.; Yamamoto, Y.; Kwak, Y. T.; Gaynor, R. B. Protein phosphatase 2C beta association with the I kappa B kinase complex is involved in regulating NF-kappa B activity J. Biol. Chem. 2004, 279 (3) 1739-1746
    • (2004) J. Biol. Chem. , vol.279 , Issue.3 , pp. 1739-1746
    • Prajapati, S.1    Verma, U.2    Yamamoto, Y.3    Kwak, Y.T.4    Gaynor, R.B.5
  • 62
    • 70350092344 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of a paired human liver healthy versus carcinoma cell lines with the same genetic background to identify potential hepatocellular carcinoma markers
    • Bao, H. M.; Song, P. M.; Liu, Q. P.; Liu, Y. K.; Yun, D.; Saiyin, H.; Du, R. Y.; Zhang, Y.; Fan, H. Z.; Yang, P. Y.; Chen, X. Quantitative proteomic analysis of a paired human liver healthy versus carcinoma cell lines with the same genetic background to identify potential hepatocellular carcinoma markers Proteomics Clin. Appl. 2009, 3 (6) 705-719
    • (2009) Proteomics Clin. Appl. , vol.3 , Issue.6 , pp. 705-719
    • Bao, H.M.1    Song, P.M.2    Liu, Q.P.3    Liu, Y.K.4    Yun, D.5    Saiyin, H.6    Du, R.Y.7    Zhang, Y.8    Fan, H.Z.9    Yang, P.Y.10    Chen, X.11
  • 63
    • 85047692516 scopus 로고    scopus 로고
    • Signalling pathways of the TNF superfamily: A double-edged sword
    • Aggarwal, B. B. Signalling pathways of the TNF superfamily: A double-edged sword Nat. Rev. Immunol. 2003, 3 (9) 745-756
    • (2003) Nat. Rev. Immunol. , vol.3 , Issue.9 , pp. 745-756
    • Aggarwal, B.B.1
  • 64
    • 14744301343 scopus 로고    scopus 로고
    • JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage
    • Yoshida, K.; Yamaguchi, T.; Natsume, T.; Kufe, D.; Miki, Y. JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage Nat. Cell Biol. 2005, 7 (3) 278-85
    • (2005) Nat. Cell Biol. , vol.7 , Issue.3 , pp. 278-285
    • Yoshida, K.1    Yamaguchi, T.2    Natsume, T.3    Kufe, D.4    Miki, Y.5
  • 65
    • 0034650872 scopus 로고    scopus 로고
    • 14-3-3 isotypes facilitate coupling of protein kinase C-zeta to Raf-1: Negative regulation by 14-3-3 phosphorylation
    • Van Der Hoeven, P. C.; Van Der Wal, J. C.; Ruurs, P.; Van Dijk, M. C.; Van Blitterswijk, J. 14-3-3 isotypes facilitate coupling of protein kinase C-zeta to Raf-1: negative regulation by 14-3-3 phosphorylation Biochem. J. 2000, 345 (2) 297-306
    • (2000) Biochem. J. , vol.345 , Issue.2 , pp. 297-306
    • Van Der Hoeven, P.C.1    Van Der Wal, J.C.2    Ruurs, P.3    Van Dijk, M.C.4    Van Blitterswijk, J.5
  • 66
    • 33646926129 scopus 로고    scopus 로고
    • 14-3-3 proteins: A historic overview
    • Aitken, A. 14-3-3 proteins: a historic overview Semin. Cancer Biol. 2006, 16 (3) 162-72
    • (2006) Semin. Cancer Biol. , vol.16 , Issue.3 , pp. 162-172
    • Aitken, A.1
  • 67
    • 0037662761 scopus 로고    scopus 로고
    • 14-3-3 Proteins find new partners in plant cell signalling
    • Roberts, M. R. 14-3-3 Proteins find new partners in plant cell signalling Trends Plant Sci. 2003, 8 (5) 218-223
    • (2003) Trends Plant Sci. , vol.8 , Issue.5 , pp. 218-223
    • Roberts, M.R.1
  • 68
    • 4143134494 scopus 로고    scopus 로고
    • Nuclear factor-[kappa]B: A friend or a foe in cancer?
    • Shishodia, S.;; Aggarwal, B. B. Nuclear factor-[kappa]B: a friend or a foe in cancer? Biochem. Pharmacol. 2004, 68 (6) 1071-1080
    • (2004) Biochem. Pharmacol. , vol.68 , Issue.6 , pp. 1071-1080
    • Shishodia, S.1    Aggarwal, B.B.2
  • 69
    • 33646363800 scopus 로고    scopus 로고
    • TAK1-mediated stress signaling pathways are essential for TNF-alpha-promoted pulmonary metastasis of murine colon cancer cells
    • Choo, M. K.; Sakurai, H.; Koizumi, K.; Saiki, I. TAK1-mediated stress signaling pathways are essential for TNF-alpha-promoted pulmonary metastasis of murine colon cancer cells Int. J. Cancer 2006, 118 (11) 2758-64
    • (2006) Int. J. Cancer , vol.118 , Issue.11 , pp. 2758-2764
    • Choo, M.K.1    Sakurai, H.2    Koizumi, K.3    Saiki, I.4
  • 70
    • 33847394078 scopus 로고    scopus 로고
    • Evidence that TNF-TNFR1-TRADD-TRAF2-RIP-TAK1-IKK pathway mediates constitutive NF-kappaB activation and proliferation in human head and neck squamous cell carcinoma
    • Jackson-Bernitsas, D. G.; Ichikawa, H.; Takada, Y.; Myers, J. N.; Lin, X. L.; Darnay, B. G.; Chaturvedi, M. M.; Aggarwal, B. B. Evidence that TNF-TNFR1-TRADD-TRAF2-RIP-TAK1-IKK pathway mediates constitutive NF-kappaB activation and proliferation in human head and neck squamous cell carcinoma Oncogene 2007, 26 (10) 1385-1397
    • (2007) Oncogene , vol.26 , Issue.10 , pp. 1385-1397
    • Jackson-Bernitsas, D.G.1    Ichikawa, H.2    Takada, Y.3    Myers, J.N.4    Lin, X.L.5    Darnay, B.G.6    Chaturvedi, M.M.7    Aggarwal, B.B.8
  • 71
  • 72
    • 0345826130 scopus 로고    scopus 로고
    • Protein phosphatase 2C{beta} association with the I{kappa}B kinase complex is involved in regulating NF-{kappa}B activity
    • Prajapati, S.; Verma, U.; Yamamoto, Y.; Kwak, Y. T.; Gaynor, R. B. Protein phosphatase 2C{beta} association with the I{kappa}B kinase complex is involved in regulating NF-{kappa}B activity J. Biol. Chem. 2004, 279 (3) 1739-1746
    • (2004) J. Biol. Chem. , vol.279 , Issue.3 , pp. 1739-1746
    • Prajapati, S.1    Verma, U.2    Yamamoto, Y.3    Kwak, Y.T.4    Gaynor, R.B.5
  • 73
    • 0036187476 scopus 로고    scopus 로고
    • TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90
    • Chen, G. Q.; Cao, P.; Goeddel, D. V. TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90 Mol. Cell 2002, 9 (2) 401-410
    • (2002) Mol. Cell , vol.9 , Issue.2 , pp. 401-410
    • Chen, G.Q.1    Cao, P.2    Goeddel, D.V.3
  • 74
    • 0033804208 scopus 로고    scopus 로고
    • Human TIP49b/RUVBL2 gene: Genomic structure, expression pattern, physical link to the human CGB/LHB gene cluster on chromosome 19q13.3
    • Parfait, B.; Giovangrandi, Y.; Asheuer, M.; Laurendeau, I.; Olivi, M.; Vodovar, N.; Vidaud, D.; Vidaud, M.; Bieche, I. Human TIP49b/RUVBL2 gene: genomic structure, expression pattern, physical link to the human CGB/LHB gene cluster on chromosome 19q13.3 Ann. Genet. 2000, 43 (2) 69-74
    • (2000) Ann. Genet. , vol.43 , Issue.2 , pp. 69-74
    • Parfait, B.1    Giovangrandi, Y.2    Asheuer, M.3    Laurendeau, I.4    Olivi, M.5    Vodovar, N.6    Vidaud, D.7    Vidaud, M.8    Bieche, I.9
  • 76
    • 0034601464 scopus 로고    scopus 로고
    • A chromatin remodelling complex involved in transcription and DNA processing
    • Shen, X. T.; Mizuguchi, G.; Hamiche, A.; Wu, C. A chromatin remodelling complex involved in transcription and DNA processing Nature 2000, 406 (6795) 541-544
    • (2000) Nature , vol.406 , Issue.6795 , pp. 541-544
    • Shen, X.T.1    Mizuguchi, G.2    Hamiche, A.3    Wu, C.4
  • 77
    • 0033529547 scopus 로고    scopus 로고
    • TIP49b, a new RuvB-like DNA helicase, is included in a complex together with another RuvB-like DNA helicase, TIP49a
    • Kanemaki, M.; Kurokawa, Y.; Matsu-ura, T.; Makino, Y.; Masani, A.; Okazaki, K.; Morishita, T.; Tamura, T. TIP49b, a new RuvB-like DNA helicase, is included in a complex together with another RuvB-like DNA helicase, TIP49a J. Biol. Chem. 1999, 274 (32) 22437-22444
    • (1999) J. Biol. Chem. , vol.274 , Issue.32 , pp. 22437-22444
    • Kanemaki, M.1    Kurokawa, Y.2    Matsu-Ura, T.3    Makino, Y.4    Masani, A.5    Okazaki, K.6    Morishita, T.7    Tamura, T.8
  • 78
    • 0034669058 scopus 로고    scopus 로고
    • Pontin52 and Reptin52 function as antagonistic regulators of beta-catenin signalling activity
    • Bauer, A.; Chauvet, S.; Huber, O.; Usseglio, F.; Rothbacher, U.; Aragnol, D.; Kemler, R.; Pradel, J. Pontin52 and Reptin52 function as antagonistic regulators of beta-catenin signalling activity EMBO J. 2000, 19 (22) 6121-6130
    • (2000) EMBO J. , vol.19 , Issue.22 , pp. 6121-6130
    • Bauer, A.1    Chauvet, S.2    Huber, O.3    Usseglio, F.4    Rothbacher, U.5    Aragnol, D.6    Kemler, R.7    Pradel, J.8
  • 79
    • 0035204479 scopus 로고    scopus 로고
    • TIP49b, a regulator of activating transcription factor 2 response to stress and DNA damage
    • Cho, S. G.; Bhoumik, A.; Broday, L.; Ivanov, V.; Rosenstein, B.; Ronai, Z. TIP49b, a regulator of activating transcription factor 2 response to stress and DNA damage Mol. Cell. Biol. 2001, 21 (24) 8398-8413
    • (2001) Mol. Cell. Biol. , vol.21 , Issue.24 , pp. 8398-8413
    • Cho, S.G.1    Bhoumik, A.2    Broday, L.3    Ivanov, V.4    Rosenstein, B.5    Ronai, Z.6
  • 80
    • 0033859666 scopus 로고    scopus 로고
    • An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc
    • Wood, M. A.; McMahon, S. B.; Cole, M. D. An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc Mol. Cell 2000, 5 (2) 321-330
    • (2000) Mol. Cell , vol.5 , Issue.2 , pp. 321-330
    • Wood, M.A.1    McMahon, S.B.2    Cole, M.D.3
  • 83
    • 0033485542 scopus 로고    scopus 로고
    • NF-kappa B activation by a signaling complex containing TRAF2, TANK and TBK1, a novel IKK-related kinase
    • Pomerantz, J. L.; Baltimore, D. NF-kappa B activation by a signaling complex containing TRAF2, TANK and TBK1, a novel IKK-related kinase EMBO J. 1999, 18 (23) 6694-6704
    • (1999) EMBO J. , vol.18 , Issue.23 , pp. 6694-6704
    • Pomerantz, J.L.1    Baltimore, D.2
  • 84
  • 85
    • 0033600604 scopus 로고    scopus 로고
    • The beginning of the end: IkappaB kinase (IKK) and NF-kappaB activation
    • Karin, M. The beginning of the end: IkappaB kinase (IKK) and NF-kappaB activation J. Biol. Chem. 1999, 274 (39) 27339-42
    • (1999) J. Biol. Chem. , vol.274 , Issue.39 , pp. 27339-27342
    • Karin, M.1
  • 88
    • 0141643193 scopus 로고    scopus 로고
    • Down-regulation of RNA helicase II/Gu results in the depletion of 18 and 28 S rRNAs in Xenopus oocyte
    • Yang, H. S.; Zhou, J. H.; Ochs, R. L.; Henning, D.; Jin, R. Y.; Valdez, B. C. Down-regulation of RNA helicase II/Gu results in the depletion of 18 and 28 S rRNAs in Xenopus oocyte J. Biol. Chem. 2003, 278 (40) 38847-38859
    • (2003) J. Biol. Chem. , vol.278 , Issue.40 , pp. 38847-38859
    • Yang, H.S.1    Zhou, J.H.2    Ochs, R.L.3    Henning, D.4    Jin, R.Y.5    Valdez, B.C.6
  • 89
    • 0347993098 scopus 로고    scopus 로고
    • Silencing of RNA helicase II/Gu alpha inhibits mammalian ribosomal RNA production
    • Henning, D.; So, R. B.; Jin, R. Y.; Lau, L. F.; Valdez, B. C. Silencing of RNA helicase II/Gu alpha inhibits mammalian ribosomal RNA production J. Biol. Chem. 2003, 278 (52) 52307-52314
    • (2003) J. Biol. Chem. , vol.278 , Issue.52 , pp. 52307-52314
    • Henning, D.1    So, R.B.2    Jin, R.Y.3    Lau, L.F.4    Valdez, B.C.5
  • 90
    • 3142579966 scopus 로고    scopus 로고
    • Identification of nucleophosmin as an NF-{kappa}B Co-activator for the induction of the human SOD2 gene
    • Dhar, S. K.; Lynn, B. C.; Daosukho, C.; St. Clair, D. K. Identification of nucleophosmin as an NF-{kappa}B Co-activator for the induction of the human SOD2 gene J. Biol. Chem. 2004, 279 (27) 28209-28219
    • (2004) J. Biol. Chem. , vol.279 , Issue.27 , pp. 28209-28219
    • Dhar, S.K.1    Lynn, B.C.2    Daosukho, C.3    St. Clair, D.K.4


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