메뉴 건너뛰기




Volumn 4, Issue 10, 2005, Pages 1569-1590

A compendium of signals and responses triggered by prodeath and prosurvival cytokines

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CELL PROTEIN; CELL RECEPTOR; CYTOKINE; EPIDERMAL GROWTH FACTOR; GUANOSINE TRIPHOSPHATASE; INSULIN; PHOSPHOTRANSFERASE; PROTEINASE; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR ALPHA;

EID: 27644496624     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M500158-MCP200     Document Type: Article
Times cited : (131)

References (67)
  • 2
    • 0037373275 scopus 로고    scopus 로고
    • Discovering genotypes underlying human phenotypes: Past successes for mendelian disease, future approaches for complex disease
    • Botstein, D., and Risch, N. (2003) Discovering genotypes underlying human phenotypes: past successes for mendelian disease, future approaches for complex disease. Nat. Genet. 33, (suppl.) 228-237
    • (2003) Nat. Genet. , vol.33 , Issue.SUPPL. , pp. 228-237
    • Botstein, D.1    Risch, N.2
  • 4
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics
    • Blagoev, B., Ong, S. E., Kratchmarova, I., and Mann, M. (2004) Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics. Nat. Biotechnol. 22, 1139-1145
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.E.2    Kratchmarova, I.3    Mann, M.4
  • 6
    • 13444278821 scopus 로고    scopus 로고
    • Reconstruction of cellular signalling networks and analysis of their properties
    • Papin, J. A., Hunter, T., Palsson, B. O., and Subramaniam, S. (2005) Reconstruction of cellular signalling networks and analysis of their properties. Nat. Rev. Mol. Cell. Biol. 6, 99-111
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 99-111
    • Papin, J.A.1    Hunter, T.2    Palsson, B.O.3    Subramaniam, S.4
  • 7
    • 0842320458 scopus 로고    scopus 로고
    • A high-throughput quantitative multiplex kinase assay for monitoring information flow in signaling networks: Application to sepsis-apoptosis
    • Janes, K. A., Albeck, J. G., Peng, L. X., Sorger, P. K., Lauffenburger, D. A., and Yaffe, M. B. (2003) A high-throughput quantitative multiplex kinase assay for monitoring information flow in signaling networks: application to sepsis-apoptosis. Mol. Cell. Proteomics 2, 463-473
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 463-473
    • Janes, K.A.1    Albeck, J.G.2    Peng, L.X.3    Sorger, P.K.4    Lauffenburger, D.A.5    Yaffe, M.B.6
  • 10
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., and Mann, M. (2003) Mass spectrometry-based proteomics. Nature 422, 198-207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 11
    • 0037418911 scopus 로고    scopus 로고
    • Informatics and quantitative analysis in biological imaging
    • Swedlow, J. R., Goldberg, I., Brauner, E., and Sorger, P. K. (2003) Informatics and quantitative analysis in biological imaging. Science 300, 100-102
    • (2003) Science , vol.300 , pp. 100-102
    • Swedlow, J.R.1    Goldberg, I.2    Brauner, E.3    Sorger, P.K.4
  • 13
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau, O., and Tschopp, J. (2003) Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114, 181-190
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 15
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis, J. M., and Avruch, J. (2001) Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol. Rev. 81, 807-869
    • (2001) Physiol. Rev. , vol.81 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 16
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-κB activity
    • Karin, M., and Ben-Neriah, Y. (2000) Phosphorylation meets ubiquitination: the control of NF-κB activity. Annu. Rev. Immunol. 18, 621-663
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 19
    • 9444287030 scopus 로고    scopus 로고
    • Common and distinct elements in cellular signaling via EGF and FGF receptors
    • Schlessinger, J. (2004) Common and distinct elements in cellular signaling via EGF and FGF receptors. Science 306, 1506-1507
    • (2004) Science , vol.306 , pp. 1506-1507
    • Schlessinger, J.1
  • 20
    • 0028157728 scopus 로고
    • The IRS-1 signaling system
    • White, M. F. (1994) The IRS-1 signaling system. Curr. Opin. Genet. Dev. 4, 47-54
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 47-54
    • White, M.F.1
  • 21
    • 17344362384 scopus 로고    scopus 로고
    • Prediction and validation of the distinct dynamics of transient and sustained ERK activation
    • Sasagawa, S., Ozaki, Y., Fujita, K., and Kuroda, S. (2005) Prediction and validation of the distinct dynamics of transient and sustained ERK activation. Nat. Cell. Biol. 7, 365-373
    • (2005) Nat. Cell. Biol. , vol.7 , pp. 365-373
    • Sasagawa, S.1    Ozaki, Y.2    Fujita, K.3    Kuroda, S.4
  • 22
    • 0037161731 scopus 로고    scopus 로고
    • Comparative assessment of large-scale data sets of protein-protein interactions
    • von Mering, C., Krause, R., Snel, B., Cornell, M., Oliver, S. G., Fields, S., and Bork, P. (2002) Comparative assessment of large-scale data sets of protein-protein interactions. Nature 417, 399-403
    • (2002) Nature , vol.417 , pp. 399-403
    • von Mering, C.1    Krause, R.2    Snel, B.3    Cornell, M.4    Oliver, S.G.5    Fields, S.6    Bork, P.7
  • 23
    • 0033552946 scopus 로고    scopus 로고
    • Robustness in bacterial chemotaxis
    • Alon, U., Surette, M. G., Barkai, N., and Leibler, S. (1999) Robustness in bacterial chemotaxis. Nature 397, 168-171
    • (1999) Nature , vol.397 , pp. 168-171
    • Alon, U.1    Surette, M.G.2    Barkai, N.3    Leibler, S.4
  • 25
    • 4544381664 scopus 로고    scopus 로고
    • Cue-signal-response analysis of TNF-induced apoptosis by partial least squares regression of dynamic multivariate data
    • Janes, K. A., Kelly, J. R., Gaudet, S., Albeck, J. G., Sorger, P. K., and Lauffenburger, D. A. (2004) Cue-signal-response analysis of TNF-induced apoptosis by partial least squares regression of dynamic multivariate data. J. Comput. Biol. 11, 544-561
    • (2004) J. Comput. Biol. , vol.11 , pp. 544-561
    • Janes, K.A.1    Kelly, J.R.2    Gaudet, S.3    Albeck, J.G.4    Sorger, P.K.5    Lauffenburger, D.A.6
  • 26
    • 0028804157 scopus 로고
    • Divergent induction of apoptosis and IL-8 secretion in HT-29 cells in response to TNF-alpha and ligation of Fas antigen
    • Abreu-Martin, M. T., Vidrich, A., Lynch, D. H., and Targan, S. R. (1995) Divergent induction of apoptosis and IL-8 secretion in HT-29 cells in response to TNF-alpha and ligation of Fas antigen. J. Immunol. 155, 4147-4154
    • (1995) J. Immunol. , vol.155 , pp. 4147-4154
    • Abreu-Martin, M.T.1    Vidrich, A.2    Lynch, D.H.3    Targan, S.R.4
  • 27
    • 0034032010 scopus 로고    scopus 로고
    • Insulin-like growth factor-I protects colon cancer cells from death factor-induced apoptosis by potentiating tumor necrosis factor α-induced mitogen-activated protein kinase and nuclear factor κB signaling pathways
    • Remacle-Bonnet, M. M., Garrouste, F. L., Heller, S., Andre, F., Marvaldi, J. L., and Pommier, G. J. (2000) Insulin-like growth factor-I protects colon cancer cells from death factor-induced apoptosis by potentiating tumor necrosis factor α-induced mitogen-activated protein kinase and nuclear factor κB signaling pathways. Cancer Res. 60, 2007-2017
    • (2000) Cancer Res. , vol.60 , pp. 2007-2017
    • Remacle-Bonnet, M.M.1    Garrouste, F.L.2    Heller, S.3    Andre, F.4    Marvaldi, J.L.5    Pommier, G.J.6
  • 28
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson, G. L., and Lapadat, R. (2002) Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 298, 1911-1912
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 29
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • Datta, S. R., Brunet, A., and Greenberg, M. E. (1999) Cellular survival: a play in three Akts. Genes Dev. 13, 2905-2927
    • (1999) Genes Dev. , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 30
    • 2942530310 scopus 로고    scopus 로고
    • ERK and p38 MAPK-activated protein kinases: A family of protein kinases with diverse biological functions
    • Roux, P. P., and Blenis, J. (2004) ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions. Microbiol. Mol. Biol. Rev. 68, 320-344
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 320-344
    • Roux, P.P.1    Blenis, J.2
  • 31
    • 0036333737 scopus 로고    scopus 로고
    • Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B
    • Scheid, M. P., Marignani, P. A., and Woodgett, J. R. (2002) Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B. Mol. Cell. Biol, 22, 6247-6260
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6247-6260
    • Scheid, M.P.1    Marignani, P.A.2    Woodgett, J.R.3
  • 32
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • Yang, J., Cron, P., Thompson, V., Good, V. M., Hess, D., Hemmings, B. A., and Barford, D. (2002) Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. Mol. Cell 9, 1227-1240
    • (2002) Mol. Cell , vol.9 , pp. 1227-1240
    • Yang, J.1    Cron, P.2    Thompson, V.3    Good, V.M.4    Hess, D.5    Hemmings, B.A.6    Barford, D.7
  • 33
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov, D. D., Guertin, D. A., Ali, S. M., and Sabatini, D. M. (2005) Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307, 1098-1101
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 34
    • 0034644523 scopus 로고    scopus 로고
    • Cellular signaling: Pivoting around PDK-1
    • Toker, A., and Newton, A. C. (2000) Cellular signaling: pivoting around PDK-1. Cell 103, 185-188
    • (2000) Cell , vol.103 , pp. 185-188
    • Toker, A.1    Newton, A.C.2
  • 36
    • 4644359805 scopus 로고    scopus 로고
    • Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase
    • Feng, J., Park, J., Cron, P., Hess, D., and Hemmings, B. A. (2004) Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase. J. Biol. Chem. 279, 41189-41196
    • (2004) J. Biol. Chem. , vol.279 , pp. 41189-41196
    • Feng, J.1    Park, J.2    Cron, P.3    Hess, D.4    Hemmings, B.A.5
  • 37
    • 0031918624 scopus 로고    scopus 로고
    • The IRS-signalling system: A network of docking proteins that mediate insulin action
    • White, M. F. (1998) The IRS-signalling system: a network of docking proteins that mediate insulin action. Mol. Cell. Biochem. 182, 3-11
    • (1998) Mol. Cell. Biochem. , vol.182 , pp. 3-11
    • White, M.F.1
  • 38
    • 11844304072 scopus 로고    scopus 로고
    • Restraining PI3K: mTOR signalling goes back to the membrane
    • Harrington, L. S., Findlay, G. M., and Lamb, R. F. (2005) Restraining PI3K: mTOR signalling goes back to the membrane. Trends Biochem. Sci. 30, 35-42
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 35-42
    • Harrington, L.S.1    Findlay, G.M.2    Lamb, R.F.3
  • 39
    • 0027437376 scopus 로고
    • Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1
    • Sun, X. J., Crimmins, D. L., Myers, M. G., Jr., Miralpeix, M., and White, M. F. (1993) Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1. Mol. Cell. Biol. 13, 7418-7428
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7418-7428
    • Sun, X.J.1    Crimmins, D.L.2    Myers Jr., M.G.3    Miralpeix, M.4    White, M.F.5
  • 40
    • 0030669392 scopus 로고    scopus 로고
    • A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation
    • Paz, K., Hemi, R., LeRoith, D., Karasik, A., Elhanany, E., Kanety, H., and Zick, Y. (1997) A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation. J. Biol. Chem. 272, 29911-29918
    • (1997) J. Biol. Chem. , vol.272 , pp. 29911-29918
    • Paz, K.1    Hemi, R.2    LeRoith, D.3    Karasik, A.4    Elhanany, E.5    Kanety, H.6    Zick, Y.7
  • 41
    • 0036710280 scopus 로고    scopus 로고
    • IRS proteins and the common path to diabetes
    • White, M. F. (2002) IRS proteins and the common path to diabetes. Am. J. Physiol. 283, E413-E422
    • (2002) Am. J. Physiol. , vol.283
    • White, M.F.1
  • 42
    • 0035099372 scopus 로고    scopus 로고
    • Association of insulin receptor substrate 1 (IRS-1) y895 with Grb-2 mediates the insulin signaling involved in IRS-1-deficient brown adipocyte mitogenesis
    • Valverde, A. M., Mur, C., Pons, S., Alvarez, A. M., White, M. F., Kahn, C. R., and Benito, M. (2001) Association of insulin receptor substrate 1 (IRS-1) y895 with Grb-2 mediates the insulin signaling involved in IRS-1-deficient brown adipocyte mitogenesis. Mol. Cell. Biol. 21, 2269-2280
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2269-2280
    • Valverde, A.M.1    Mur, C.2    Pons, S.3    Alvarez, A.M.4    White, M.F.5    Kahn, C.R.6    Benito, M.7
  • 43
    • 0035169995 scopus 로고    scopus 로고
    • Involvement of insulin receptor substrates in epidermal growth factor induced activation of phosphatidylinositol 3-kinase in rat hepatocyte primary culture
    • Fujioka, T., and Ui, M. (2001) Involvement of insulin receptor substrates in epidermal growth factor induced activation of phosphatidylinositol 3-kinase in rat hepatocyte primary culture. Eur. J. Biochem. 268, 25-34
    • (2001) Eur. J. Biochem. , vol.268 , pp. 25-34
    • Fujioka, T.1    Ui, M.2
  • 44
    • 0034826541 scopus 로고    scopus 로고
    • Further evidence for the involvement of insulin receptor substrates in epidermal growth factor-induced activation of phosphatidylinositol 3-kinase
    • Fujioka, T., Kim, J. H., Adachi, H., Saito, K., Tsujimoto, M., Yokoyama, S., and Ui, M. (2001) Further evidence for the involvement of insulin receptor substrates in epidermal growth factor-induced activation of phosphatidylinositol 3-kinase. Eur. J. Biochem. 268, 4158-4168
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4158-4168
    • Fujioka, T.1    Kim, J.H.2    Adachi, H.3    Saito, K.4    Tsujimoto, M.5    Yokoyama, S.6    Ui, M.7
  • 45
    • 0037183974 scopus 로고    scopus 로고
    • Epidermal growth factor and transforming growth factor α mimic the effects of insulin in human fat cells and augment downstream signaling in insulin resistance
    • Gogg, S., and Smith, U. (2002) Epidermal growth factor and transforming growth factor α mimic the effects of insulin in human fat cells and augment downstream signaling in insulin resistance. J. Biol. Chem. 277, 36045-36051
    • (2002) J. Biol. Chem. , vol.277 , pp. 36045-36051
    • Gogg, S.1    Smith, U.2
  • 46
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer, J. C., Cantley, L. C., and Yaffe, M. B. (2003) Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res. 31, 3635-3641
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 47
    • 26444453273 scopus 로고    scopus 로고
    • Fully automated synthesis of (phospho)peptide arrays in microtiter plate wells provides efficient access to protein tyrosine kinase characterization
    • Saxinger, C., Conrads, T. P., Goldstein, D. J., and Veenstra, T. D. (2005) Fully automated synthesis of (phospho)peptide arrays in microtiter plate wells provides efficient access to protein tyrosine kinase characterization. BMC Immunol. 6, 1
    • (2005) BMC Immunol. , vol.6 , pp. 1
    • Saxinger, C.1    Conrads, T.P.2    Goldstein, D.J.3    Veenstra, T.D.4
  • 49
    • 0035072833 scopus 로고    scopus 로고
    • A motif-based profile scanning approach for genome-wide prediction of signaling pathways
    • Yaffe, M. B., Leparc, G. G., Lai, J., Obata, T., Volinia, S., and Cantley, L. C. (2001) A motif-based profile scanning approach for genome-wide prediction of signaling pathways. Nat. Biotechnol. 19, 348-353
    • (2001) Nat. Biotechnol. , vol.19 , pp. 348-353
    • Yaffe, M.B.1    Leparc, G.G.2    Lai, J.3    Obata, T.4    Volinia, S.5    Cantley, L.C.6
  • 50
    • 0031919552 scopus 로고    scopus 로고
    • Insulin signal transduction through protein kinase cascades
    • Avruch, J. (1998) Insulin signal transduction through protein kinase cascades. Mol. Cell. Biochem. 182, 31-48
    • (1998) Mol. Cell. Biochem. , vol.182 , pp. 31-48
    • Avruch, J.1
  • 51
    • 0039425278 scopus 로고    scopus 로고
    • Negative regulation of the forkhead transcription factor FKHR by Akt
    • Tang, E. D., Nunez, G., Barr, F. G., and Guan, K. L. (1999) Negative regulation of the forkhead transcription factor FKHR by Akt. J. Biol. Chem. 274, 16741-16746
    • (1999) J. Biol. Chem. , vol.274 , pp. 16741-16746
    • Tang, E.D.1    Nunez, G.2    Barr, F.G.3    Guan, K.L.4
  • 52
    • 0033546439 scopus 로고    scopus 로고
    • Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B
    • Rena, G., Guo, S., Cichy, S. C., Unterman, T. G., and Cohen, P. (1999) Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B. J. Biol. Chem. 274, 17179-17183
    • (1999) J. Biol. Chem. , vol.274 , pp. 17179-17183
    • Rena, G.1    Guo, S.2    Cichy, S.C.3    Unterman, T.G.4    Cohen, P.5
  • 53
    • 0030951346 scopus 로고    scopus 로고
    • Insulin activates protein kinase B, inhibits glycogen synthase kinase-3 and activates glycogen synthase by rapamycin-insensitive pathways in skeletal muscle and adipose tissue
    • Cross, D. A., Watt, P. W., Shaw, M., van der Kaay, J., Downes, C. P., Holder, J. C., and Cohen, P. (1997) Insulin activates protein kinase B, inhibits glycogen synthase kinase-3 and activates glycogen synthase by rapamycin-insensitive pathways in skeletal muscle and adipose tissue. FEBS Lett. 406, 211-215
    • (1997) FEBS Lett. , vol.406 , pp. 211-215
    • Cross, D.A.1    Watt, P.W.2    Shaw, M.3    van der Kaay, J.4    Downes, C.P.5    Holder, J.C.6    Cohen, P.7
  • 54
    • 0033522897 scopus 로고    scopus 로고
    • Insulin stimulates phosphorylation of the forkhead transcription factor FKHR on serine 253 through a Wortmannin-sensitive pathway
    • Nakae, J., Park, B. C., and Accili, D. (1999) Insulin stimulates phosphorylation of the forkhead transcription factor FKHR on serine 253 through a Wortmannin-sensitive pathway. J. Biol. Chem. 274, 15982-15985
    • (1999) J. Biol. Chem. , vol.274 , pp. 15982-15985
    • Nakae, J.1    Park, B.C.2    Accili, D.3
  • 55
    • 0035797921 scopus 로고    scopus 로고
    • Insulin regulation of gene expression through the forkhead transcription factor Foxo1 (Fkhr) requires kinases distinct from Akt
    • Nakae, J., Kitamura, T., Ogawa, W., Kasuga, M., and Accili, D. (2001) Insulin regulation of gene expression through the forkhead transcription factor Foxo1 (Fkhr) requires kinases distinct from Akt. Biochemistry 40, 11768-11776
    • (2001) Biochemistry , vol.40 , pp. 11768-11776
    • Nakae, J.1    Kitamura, T.2    Ogawa, W.3    Kasuga, M.4    Accili, D.5
  • 56
    • 0035135841 scopus 로고    scopus 로고
    • Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOX03a)
    • Brunet, A., Park, J., Tran, H., Hu, L. S., Hemmings, B. A., and Greenberg, M. E. (2001) Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOX03a). Mol. Cell. Biol. 21, 952-965
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 952-965
    • Brunet, A.1    Park, J.2    Tran, H.3    Hu, L.S.4    Hemmings, B.A.5    Greenberg, M.E.6
  • 57
    • 11144325691 scopus 로고
    • Partial least-squares regression - A tutorial
    • Geladi, P., and Kowalski, B. R. (1986) Partial least-squares regression - a tutorial. Anal. Chim. Acta 185, 1-17
    • (1986) Anal. Chim. Acta , vol.185 , pp. 1-17
    • Geladi, P.1    Kowalski, B.R.2
  • 58
    • 0028354319 scopus 로고
    • Exponentially weighted moving principal components - Analysis and projections to latent structures
    • Wold, S. (1994) Exponentially weighted moving principal components - analysis and projections to latent structures. Chemom. Intell. Lab. Syst. 23, 149-161
    • (1994) Chemom. Intell. Lab. Syst. , vol.23 , pp. 149-161
    • Wold, S.1
  • 59
    • 0020933452 scopus 로고
    • Biological effects in vitro of monoclonal antibodies to human epidermal growth factor receptors
    • Sato, J. D., Kawamoto, T., Le, A. D., Mendelsohn, J., Polikoff, J., and Sato, G. H. (1983) Biological effects in vitro of monoclonal antibodies to human epidermal growth factor receptors. Mol. Biol. Med. 1, 511-529
    • (1983) Mol. Biol. Med. , vol.1 , pp. 511-529
    • Sato, J.D.1    Kawamoto, T.2    Le, A.D.3    Mendelsohn, J.4    Polikoff, J.5    Sato, G.H.6
  • 60
    • 0034618862 scopus 로고    scopus 로고
    • The role of the interleukin-1-receptor antagonist in blocking inflammation mediated by interleukin-1
    • Dinarello, C. A. (2000) The role of the interleukin-1-receptor antagonist in blocking inflammation mediated by interleukin-1. N. Engl. J. Med. 343, 732-734
    • (2000) N. Engl. J. Med. , vol.343 , pp. 732-734
    • Dinarello, C.A.1
  • 61
    • 0035863514 scopus 로고    scopus 로고
    • Assessment of tumor necrosis factor receptor and Fas signaling pathways by transcriptional profiling
    • Manos, E. J., and Jones, D. A. (2001) Assessment of tumor necrosis factor receptor and Fas signaling pathways by transcriptional profiling. Cancer Res. 61, 433-438
    • (2001) Cancer Res. , vol.61 , pp. 433-438
    • Manos, E.J.1    Jones, D.A.2
  • 62
    • 9244224723 scopus 로고    scopus 로고
    • Intrinsic tumour suppression
    • Lowe, S. W., Cepero, E., and Evan, G. (2004) Intrinsic tumour suppression. Nature 432, 307-315
    • (2004) Nature , vol.432 , pp. 307-315
    • Lowe, S.W.1    Cepero, E.2    Evan, G.3
  • 63
    • 0344875667 scopus 로고    scopus 로고
    • Proteomics. Public projects gear up to chart the protein landscape
    • Service, R. F. (2003) Proteomics. Public projects gear up to chart the protein landscape. Science 302, 1316-1318
    • (2003) Science , vol.302 , pp. 1316-1318
    • Service, R.F.1
  • 64
    • 2342633297 scopus 로고    scopus 로고
    • Protein arrays: Proteomics in multiplex
    • Melton, L. (2004) Protein arrays: proteomics in multiplex. Nature 429, 101-107
    • (2004) Nature , vol.429 , pp. 101-107
    • Melton, L.1
  • 65
    • 0036181363 scopus 로고    scopus 로고
    • Regulation of stress-activated protein kinase signaling pathways by protein phosphatases
    • Tamura, S., Hanada, M., Ohnishi, M., Katsura, K., Sasaki, M., and Kobayashi, T. (2002) Regulation of stress-activated protein kinase signaling pathways by protein phosphatases. Eur. J. Biochem. 269, 1060-1066
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1060-1066
    • Tamura, S.1    Hanada, M.2    Ohnishi, M.3    Katsura, K.4    Sasaki, M.5    Kobayashi, T.6
  • 66
    • 0003009442 scopus 로고    scopus 로고
    • Multiway calibration. Multilinear PLS
    • Bro, R. (1996) Multiway calibration. Multilinear PLS. J. Chemom. 10, 47-61
    • (1996) J. Chemom. , vol.10 , pp. 47-61
    • Bro, R.1
  • 67
    • 0034712843 scopus 로고    scopus 로고
    • Robust perfect adaptation in bacterial chemotaxis through integral feedback control
    • Yi, T. M., Huang, Y., Simon, M. I., and Doyle, J. (2000) Robust perfect adaptation in bacterial chemotaxis through integral feedback control. Proc. Natl. Acad. Sci. U. S. A. 97, 4649-4653
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4649-4653
    • Yi, T.M.1    Huang, Y.2    Simon, M.I.3    Doyle, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.