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Volumn 32, Issue 1, 2007, Pages 61-70

FER as a novel target for cancer therapy

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; BETA CATENIN; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEIN FER; PROTEIN TYROSINE KINASE; STAT3 PROTEIN; UNCLASSIFIED DRUG;

EID: 34247635155     PISSN: 03778282     EISSN: None     Source Type: Journal    
DOI: 10.1358/dof.2007.032.01.1065737     Document Type: Review
Times cited : (2)

References (90)
  • 1
    • 0024233115 scopus 로고
    • Novel protein-tyrosine kinase cDNAs related to fps/fes and eph cloned using antiphosphotyrosine antibody
    • Letwin, K., Yee, S.-P., Pawson, T. Novel protein-tyrosine kinase cDNAs related to fps/fes and eph cloned using antiphosphotyrosine antibody. Oncogene 1988, 3: 621-7.
    • (1988) Oncogene , vol.3 , pp. 621-627
    • Letwin, K.1    Yee, S.-P.2    Pawson, T.3
  • 2
    • 0024500460 scopus 로고
    • Isolation and sequence analysis of a novel human tyrosine kinase gene
    • Hao, Q.-L., Heisterkamp, N., Groffen, J. Isolation and sequence analysis of a novel human tyrosine kinase gene. Mol Cell Biol 1989, 9: 1587-93.
    • (1989) Mol Cell Biol , vol.9 , pp. 1587-1593
    • Hao, Q.-L.1    Heisterkamp, N.2    Groffen, J.3
  • 4
    • 0036273766 scopus 로고    scopus 로고
    • Closing in on the biological functions of Fps/Fes and Fer
    • Greer, P. Closing in on the biological functions of Fps/Fes and Fer. Nat Rev Mol Cell Biol 2002, 3: 278-89.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 278-289
    • Greer, P.1
  • 5
    • 0032483517 scopus 로고    scopus 로고
    • Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the cytoplasmic tyrosine kinase FER
    • Kim, L., Wong, TW. Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the cytoplasmic tyrosine kinase FER. J Biol Chem 1998, 273: 23542-8.
    • (1998) J Biol Chem , vol.273 , pp. 23542-23548
    • Kim, L.1    Wong, T.W.2
  • 6
    • 0028881801 scopus 로고
    • Temporal activation of nontransmembrane protein-tyrosine kinases following mast cell Fc epsilon RI engagement
    • Penhallow, R.C., Class, K., Sonoda, H., Bolen, J.B., Rowley, R.B. Temporal activation of nontransmembrane protein-tyrosine kinases following mast cell Fc epsilon RI engagement. J Biol Chem 1995, 270: 23362-5.
    • (1995) J Biol Chem , vol.270 , pp. 23362-23365
    • Penhallow, R.C.1    Class, K.2    Sonoda, H.3    Bolen, J.B.4    Rowley, R.B.5
  • 7
    • 0036724531 scopus 로고    scopus 로고
    • Fer kinase is required for sustained p38 kinase activation and maximal chemotaxis of activated mast cells
    • Craig, A.W., Greer, P.A. Fer kinase is required for sustained p38 kinase activation and maximal chemotaxis of activated mast cells. Mol Cell Biol 2002, 22: 6363-74.
    • (2002) Mol Cell Biol , vol.22 , pp. 6363-6374
    • Craig, A.W.1    Greer, P.A.2
  • 8
    • 0141632825 scopus 로고    scopus 로고
    • Identification of Fer tyrosine kinase localized on microtubules as a platelet endothelial cell adhesion molecule-1 phosphorylating kinase in vascular endothelial cells
    • Kogata, N., Masuda, M., Kamioka, Y. et al. Identification of Fer tyrosine kinase localized on microtubules as a platelet endothelial cell adhesion molecule-1 phosphorylating kinase in vascular endothelial cells. Mol Biol Cell 2003, 14: 3553-64.
    • (2003) Mol Biol Cell , vol.14 , pp. 3553-3564
    • Kogata, N.1    Masuda, M.2    Kamioka, Y.3
  • 9
    • 0141529737 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of plakoglobin causes contrary effects on its association with desmosomes and adherens junction components and modulates β-catenin-mediated transcription
    • Miravet, S., Piedra, J., Castano, J. et al. Tyrosine phosphorylation of plakoglobin causes contrary effects on its association with desmosomes and adherens junction components and modulates β-catenin-mediated transcription. Mol Cell Biol 2003, 23: 7391-402.
    • (2003) Mol Cell Biol , vol.23 , pp. 7391-7402
    • Miravet, S.1    Piedra, J.2    Castano, J.3
  • 10
    • 0037378505 scopus 로고    scopus 로고
    • p120 Catenin-associated Fer and Fyn tyrosine kinases regulate β-catenin Tyr-142 phosphorylation and β-catenin-α-catenin interaction
    • Piedra, J., Miravet, S., Castano, J. et al. p120 Catenin-associated Fer and Fyn tyrosine kinases regulate β-catenin Tyr-142 phosphorylation and β-catenin-α-catenin interaction. Mol Cell Biol 2003, 23: 2287-97.
    • (2003) Mol Cell Biol , vol.23 , pp. 2287-2297
    • Piedra, J.1    Miravet, S.2    Castano, J.3
  • 12
    • 0034672015 scopus 로고    scopus 로고
    • The protein-tyrosine kinase fer associates with signaling complexes containing insulin receptor substrate-1 and phosphatidylinositol 3-kinase
    • Iwanishi, M., Czech, M.P., Cherniack, A.D. The protein-tyrosine kinase fer associates with signaling complexes containing insulin receptor substrate-1 and phosphatidylinositol 3-kinase. J Biol Chem 2000, 275: 38995-9000.
    • (2000) J Biol Chem , vol.275 , pp. 38995-39000
    • Iwanishi, M.1    Czech, M.P.2    Cherniack, A.D.3
  • 13
    • 0034666009 scopus 로고    scopus 로고
    • FER kinase activation of STAT3 is determined by the N-terminal sequence
    • Priel-Halachmi, S., Ben-Dor, I., Shpungin, S. et al. FER kinase activation of STAT3 is determined by the N-terminal sequence. J Biol Chem 2000, 275: 28902-10.
    • (2000) J Biol Chem , vol.275 , pp. 28902-28910
    • Priel-Halachmi, S.1    Ben-Dor, I.2    Shpungin, S.3
  • 14
    • 0036385851 scopus 로고    scopus 로고
    • Direct binding of plectin to Fer kinase and negative regulation of its catalytic activity
    • Lunter, P.C., Wiche, G. Direct binding of plectin to Fer kinase and negative regulation of its catalytic activity. Biochem Biophys Res Commun 2002, 296: 904-10.
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 904-910
    • Lunter, P.C.1    Wiche, G.2
  • 15
    • 0035160210 scopus 로고    scopus 로고
    • Mice devoid of fer protein-tyrosine kinase activity are viable and fertile but display reduced cortactin phosphorylation
    • Craig, A.W., Zirngibl, R., Williams, K., Cole, L.A., Greer, P.A. Mice devoid of fer protein-tyrosine kinase activity are viable and fertile but display reduced cortactin phosphorylation. Mol Cell Biol 2001, 21: 603-13.
    • (2001) Mol Cell Biol , vol.21 , pp. 603-613
    • Craig, A.W.1    Zirngibl, R.2    Williams, K.3    Cole, L.A.4    Greer, P.A.5
  • 16
    • 0032717925 scopus 로고    scopus 로고
    • Targeted disruption of the murine fps/fes proto-oncogene reveals that Fps/Fes kinase activity is dispensable for hematopoiesis
    • Senis, Y., Zirngibl, R., McVeigh, J., Haman, A., Hoang, T., Greer, P.A. Targeted disruption of the murine fps/fes proto-oncogene reveals that Fps/Fes kinase activity is dispensable for hematopoiesis. Mol Cell Biol 1999, 19: 7436-46.
    • (1999) Mol Cell Biol , vol.19 , pp. 7436-7446
    • Senis, Y.1    Zirngibl, R.2    McVeigh, J.3    Haman, A.4    Hoang, T.5    Greer, P.A.6
  • 17
    • 0024369295 scopus 로고
    • Lymphoid and mesenchymal tumors in transgenic mice expressing the v-fps protein-tyrosine kinase
    • Yee, S.P., Mock, D., Greer, P. et al. Lymphoid and mesenchymal tumors in transgenic mice expressing the v-fps protein-tyrosine kinase. Mol Cell Biol 1989, 9: 5491-9.
    • (1989) Mol Cell Biol , vol.9 , pp. 5491-5499
    • Yee, S.P.1    Mock, D.2    Greer, P.3
  • 19
    • 33646830138 scopus 로고    scopus 로고
    • A growth-suppressive function for the c-fes protein-tyrosine kinase in colorectal cancer
    • Delfino, F.J., Stevenson, H., Smithgall, T.E. A growth-suppressive function for the c-fes protein-tyrosine kinase in colorectal cancer. J Biol Chem 2006, 281: 8829-35.
    • (2006) J Biol Chem , vol.281 , pp. 8829-8835
    • Delfino, F.J.1    Stevenson, H.2    Smithgall, T.E.3
  • 20
    • 0037173762 scopus 로고    scopus 로고
    • Gamma interferon down-regulates Fer and induces its association with inactive STAT3 in colon carcinoma cells
    • Orlovsky, K., Theodor, L., Malovani, H., Chowers, Y., Nir, U. Gamma interferon down-regulates Fer and induces its association with inactive STAT3 in colon carcinoma cells. Oncogene 2002, 21: 4997-5001.
    • (2002) Oncogene , vol.21 , pp. 4997-5001
    • Orlovsky, K.1    Theodor, L.2    Malovani, H.3    Chowers, Y.4    Nir, U.5
  • 21
    • 0033968740 scopus 로고    scopus 로고
    • Links between Fer tyrosine kinase expression levels and prostate cell proliferation
    • Allard, P., Zoubeidi, A., Nguyen, L.T. et al. Links between Fer tyrosine kinase expression levels and prostate cell proliferation. Mol Cell Endocrinol 2000, 159: 63-77.
    • (2000) Mol Cell Endocrinol , vol.159 , pp. 63-77
    • Allard, P.1    Zoubeidi, A.2    Nguyen, L.T.3
  • 22
    • 33746054141 scopus 로고    scopus 로고
    • Downregulation of Fer induces PP1 activation and cell-cycle arrest in malignant cells
    • Pasder, O., Shpungin, S., Salem, Y. et al. Downregulation of Fer induces PP1 activation and cell-cycle arrest in malignant cells. Oncogene 2006, 25: 4194-206.
    • (2006) Oncogene , vol.25 , pp. 4194-4206
    • Pasder, O.1    Shpungin, S.2    Salem, Y.3
  • 23
    • 0041765788 scopus 로고    scopus 로고
    • Fer is a downstream effector of insulin and mediates the activation of signal transducer and activator of transcription 3 in myogenic cells
    • Taler, M., Shpungin, S., Salem, Y., Malovani, H., Pasder, O., Nir, U. Fer is a downstream effector of insulin and mediates the activation of signal transducer and activator of transcription 3 in myogenic cells. Mol Endocrinol 2003, 17: 1580-92.
    • (2003) Mol Endocrinol , vol.17 , pp. 1580-1592
    • Taler, M.1    Shpungin, S.2    Salem, Y.3    Malovani, H.4    Pasder, O.5    Nir, U.6
  • 24
    • 0019133661 scopus 로고
    • Mutations affecting segment number and polarity in Drosophila
    • Nusslein-Volhard, C., Wieschaus, E. Mutations affecting segment number and polarity in Drosophila. Nature 1980, 287: 795-801.
    • (1980) Nature , vol.287 , pp. 795-801
    • Nusslein-Volhard, C.1    Wieschaus, E.2
  • 25
    • 0037459077 scopus 로고    scopus 로고
    • Sticky business: Orchestrating cellular signals at adherens junctions
    • Perez-Moreno, M., Jamora, C., Fuchs, E. Sticky business: Orchestrating cellular signals at adherens junctions. Cell 2003, 112: 535-48.
    • (2003) Cell , vol.112 , pp. 535-548
    • Perez-Moreno, M.1    Jamora, C.2    Fuchs, E.3
  • 26
    • 1542347695 scopus 로고    scopus 로고
    • Convergence of Wnt, β-catenin, and cadherin pathways
    • Nelson, W.J., Nusse, R. Convergence of Wnt, β-catenin, and cadherin pathways. Science 2004, 303: 1483-7.
    • (2004) Science , vol.303 , pp. 1483-1487
    • Nelson, W.J.1    Nusse, R.2
  • 27
    • 0033545845 scopus 로고    scopus 로고
    • The cyclin D1 gene is a target of the β-catenin/LEF-1 pathway
    • Shtutman, M., Zhurinsky, J., Simcha, I. et al. The cyclin D1 gene is a target of the β-catenin/LEF-1 pathway. Proc Natl Acad Sci USA 1999, 96: 5522-7.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5522-5527
    • Shtutman, M.1    Zhurinsky, J.2    Simcha, I.3
  • 28
    • 0035300492 scopus 로고    scopus 로고
    • Increased β-catenin expression and nuclear translocation accompany cellular hyperproliferation in vivo
    • Sellin, J.H., Umar, S., Xiao, J., Morris, A.P. Increased β-catenin expression and nuclear translocation accompany cellular hyperproliferation in vivo. Cancer Res 2001, 61: 2899-906.
    • (2001) Cancer Res , vol.61 , pp. 2899-2906
    • Sellin, J.H.1    Umar, S.2    Xiao, J.3    Morris, A.P.4
  • 29
    • 0038359353 scopus 로고    scopus 로고
    • Caught up in a Wnt storm: Wnt signaling in cancer
    • Giles, R.H., van Es, J.H., Clevers, H. Caught up in a Wnt storm: Wnt signaling in cancer. Biochim Biophys Acta 2003, 1653: 1-24.
    • (2003) Biochim Biophys Acta , vol.1653 , pp. 1-24
    • Giles, R.H.1    van Es, J.H.2    Clevers, H.3
  • 30
    • 4344618740 scopus 로고    scopus 로고
    • Continuous association of Cadherin with β-catenin requires the non-receptor tyrosine-kinase Fer
    • Xu, G., Craig, A.W., Greer, P. et al. Continuous association of Cadherin with β-catenin requires the non-receptor tyrosine-kinase Fer. J Cell Sci 2004, 117: 3207-19.
    • (2004) J Cell Sci , vol.117 , pp. 3207-3219
    • Xu, G.1    Craig, A.W.2    Greer, P.3
  • 31
    • 0033968740 scopus 로고    scopus 로고
    • Links between Fer tyrosine kinase expression levels and prostate cell proliferation
    • Allard, P., Zoubeidi, A., Nguyen, L. T. et al. Links between Fer tyrosine kinase expression levels and prostate cell proliferation. Mol Cell Endocrinol 2000, 159: 63-77.
    • (2000) Mol Cell Endocrinol , vol.159 , pp. 63-77
    • Allard, P.1    Zoubeidi, A.2    Nguyen, L.T.3
  • 32
    • 0034641679 scopus 로고    scopus 로고
    • N-terminal sequences direct the autophosphorylation states of the FER tyrosine kinases in vivo
    • Orlovsky, K., Ben-Dor, I., Priel-Halachmi, S., Malovany, H., Nir, U. N-terminal sequences direct the autophosphorylation states of the FER tyrosine kinases in vivo. Biochemistry 2000, 39: 11084-91.
    • (2000) Biochemistry , vol.39 , pp. 11084-11091
    • Orlovsky, K.1    Ben-Dor, I.2    Priel-Halachmi, S.3    Malovany, H.4    Nir, U.5
  • 33
    • 33748047128 scopus 로고    scopus 로고
    • RB and cell cycle progression
    • Giacinti, C., Giordano, A. RB and cell cycle progression. Oncogene 2006, 25: 5220-7.
    • (2006) Oncogene , vol.25 , pp. 5220-5227
    • Giacinti, C.1    Giordano, A.2
  • 34
    • 33748028804 scopus 로고    scopus 로고
    • Cell cycle control and beyond: Emerging roles for the retinoblastoma gene family
    • Genovese, C., Trani, D., Caputi, M., Claudio, P.P. Cell cycle control and beyond: Emerging roles for the retinoblastoma gene family. Oncogene 2006, 25: 5201-9.
    • (2006) Oncogene , vol.25 , pp. 5201-5209
    • Genovese, C.1    Trani, D.2    Caputi, M.3    Claudio, P.P.4
  • 35
    • 0001510491 scopus 로고    scopus 로고
    • The RB and p53 pathways in cancer
    • Sherr, C.J., McCormick, F. The RB and p53 pathways in cancer. Cancer Cell 2002, 2: 103-12.
    • (2002) Cancer Cell , vol.2 , pp. 103-112
    • Sherr, C.J.1    McCormick, F.2
  • 36
    • 0026538337 scopus 로고
    • The retinoblastoma protein and cell cycle regulation
    • Hamel, P.A., Gallie, B.L., Phillips, R.A. The retinoblastoma protein and cell cycle regulation. Trends Genet 1992, 8: 180-5.
    • (1992) Trends Genet , vol.8 , pp. 180-185
    • Hamel, P.A.1    Gallie, B.L.2    Phillips, R.A.3
  • 37
    • 0026636908 scopus 로고
    • Retinoblastoma protein switches the E2F site from positive to negative element
    • Weintraub, S.J., Prater, C.A., Dean, D.C. Retinoblastoma protein switches the E2F site from positive to negative element. Nature 1992, 358: 259-61.
    • (1992) Nature , vol.358 , pp. 259-261
    • Weintraub, S.J.1    Prater, C.A.2    Dean, D.C.3
  • 38
    • 0032484989 scopus 로고    scopus 로고
    • Retinoblastoma protein recruits histone deacetylase to repress transcription
    • Brehm, A., Miska, E.A., McCance, D.J., Reid, J.L., Bannister, A.J., Kouzarides, T. Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature 1998, 391: 597-601.
    • (1998) Nature , vol.391 , pp. 597-601
    • Brehm, A.1    Miska, E.A.2    McCance, D.J.3    Reid, J.L.4    Bannister, A.J.5    Kouzarides, T.6
  • 39
    • 0032549001 scopus 로고    scopus 로고
    • Rb interacts with histone deacetylase to repress transcription
    • Luo, R.X., Postigo, A.A., Dean, D.C. Rb interacts with histone deacetylase to repress transcription. Cell 1998, 92: 463-73.
    • (1998) Cell , vol.92 , pp. 463-473
    • Luo, R.X.1    Postigo, A.A.2    Dean, D.C.3
  • 40
    • 0032484904 scopus 로고    scopus 로고
    • Retinoblastoma protein represses transcription by recruiting a histone deacetylase
    • Magnaghi-Jaulin, L., Groisman, R., Naguibneva, I. et al. Retinoblastoma protein represses transcription by recruiting a histone deacetylase. Nature 1998, 391: 601-5.
    • (1998) Nature , vol.391 , pp. 601-605
    • Magnaghi-Jaulin, L.1    Groisman, R.2    Naguibneva, I.3
  • 41
    • 0034964014 scopus 로고    scopus 로고
    • Retinoblastoma protein partners
    • Morris, E.J., Dyson, N.J. Retinoblastoma protein partners. Adv Cancer Res 2001, 82: 1-54.
    • (2001) Adv Cancer Res , vol.82 , pp. 1-54
    • Morris, E.J.1    Dyson, N.J.2
  • 42
    • 0032146274 scopus 로고    scopus 로고
    • The regulation of E2F by pRB-family proteins
    • Dyson, N. The regulation of E2F by pRB-family proteins. Genes Dev 1998, 12: 2245-62.
    • (1998) Genes Dev , vol.12 , pp. 2245-2262
    • Dyson, N.1
  • 43
    • 33748075785 scopus 로고    scopus 로고
    • The retinoblastoma tumor-suppressor gene, the exception that proves the rule
    • Goodrich, D.W. The retinoblastoma tumor-suppressor gene, the exception that proves the rule. Oncogene 2006, 25: 5233-43.
    • (2006) Oncogene , vol.25 , pp. 5233-5243
    • Goodrich, D.W.1
  • 44
    • 0038052805 scopus 로고    scopus 로고
    • The cell cycle: A review of regulation, deregulation and therapeutic targets in cancer
    • Vermeulen, K., Van Bockstaele, D.R., Berneman, Z.N. The cell cycle: A review of regulation, deregulation and therapeutic targets in cancer. Cell Prolif 2003, 36: 131-49.
    • (2003) Cell Prolif , vol.36 , pp. 131-149
    • Vermeulen, K.1    Van Bockstaele, D.R.2    Berneman, Z.N.3
  • 46
    • 0041854279 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 2 is essential for meiosis but not for mitotic cell division in mice
    • Ortega, S., Prieto, I., Odajima, J. et al. Cyclin-dependent kinase 2 is essential for meiosis but not for mitotic cell division in mice. Nat Genet 2003, 35: 25-31.
    • (2003) Nat Genet , vol.35 , pp. 25-31
    • Ortega, S.1    Prieto, I.2    Odajima, J.3
  • 47
    • 0041327168 scopus 로고    scopus 로고
    • Proliferation of cancer cells despite CDK2 inhibition
    • Tetsu, O., McCormick, F. Proliferation of cancer cells despite CDK2 inhibition. Cancer Cell 2003, 3: 233-45.
    • (2003) Cancer Cell , vol.3 , pp. 233-245
    • Tetsu, O.1    McCormick, F.2
  • 48
    • 4444247138 scopus 로고    scopus 로고
    • Mammalian cells cycle without the D-type cyclin-dependent kinases Cdk4 and Cdk6
    • Malumbres, M., Sotillo, R., Santamaria, D. et al. Mammalian cells cycle without the D-type cyclin-dependent kinases Cdk4 and Cdk6. Cell 2004, 118: 493-504.
    • (2004) Cell , vol.118 , pp. 493-504
    • Malumbres, M.1    Sotillo, R.2    Santamaria, D.3
  • 49
    • 8644219655 scopus 로고    scopus 로고
    • Living with or without cyclins and cyclin-dependent kinases
    • Sherr, C.J., Roberts, J.M. Living with or without cyclins and cyclin-dependent kinases. Genes Dev 2004, 18: 2699-711.
    • (2004) Genes Dev , vol.18 , pp. 2699-2711
    • Sherr, C.J.1    Roberts, J.M.2
  • 50
    • 12644284504 scopus 로고    scopus 로고
    • The consensus motif for phosphorylation by cyclin D1-Cdk4 is different from that for phosphorylation by cyclin A/E-Cdk2
    • Kitagawa, M., Higashi, H., Jung, H.K. et al. The consensus motif for phosphorylation by cyclin D1-Cdk4 is different from that for phosphorylation by cyclin A/E-Cdk2. EMBO J 1996, 15: 7060-9.
    • (1996) EMBO J , vol.15 , pp. 7060-7069
    • Kitagawa, M.1    Higashi, H.2    Jung, H.K.3
  • 51
    • 0031019197 scopus 로고    scopus 로고
    • Cyclin D1/Cdk4 regulates retinoblastoma protein-mediated cell cycle arrest by site-specific phosphorylation
    • Connell-Crowley, L., Harper, J.W., Goodrich, D.W. Cyclin D1/Cdk4 regulates retinoblastoma protein-mediated cell cycle arrest by site-specific phosphorylation. Mol Biol Cell 1997, 8: 287-301.
    • (1997) Mol Biol Cell , vol.8 , pp. 287-301
    • Connell-Crowley, L.1    Harper, J.W.2    Goodrich, D.W.3
  • 52
    • 0030918714 scopus 로고    scopus 로고
    • Differential phosphorylation of the retinoblastoma protein by G1/S cyclin-dependent kinases
    • Zarkowska, T., Mittnacht, S. Differential phosphorylation of the retinoblastoma protein by G1/S cyclin-dependent kinases. J Biol Chem 1997, 272: 12738-46.
    • (1997) J Biol Chem , vol.272 , pp. 12738-12746
    • Zarkowska, T.1    Mittnacht, S.2
  • 53
    • 0035959632 scopus 로고    scopus 로고
    • Protein phosphatase 1α-mediated stimulation of apoptosis is associated with dephosphorylation of the retinoblastoma protein
    • Wang, R.H., Liu, C.W., Avramis, V.I., Berndt, N. Protein phosphatase 1α-mediated stimulation of apoptosis is associated with dephosphorylation of the retinoblastoma protein. Oncogene 2001, 20: 6111-22.
    • (2001) Oncogene , vol.20 , pp. 6111-6122
    • Wang, R.H.1    Liu, C.W.2    Avramis, V.I.3    Berndt, N.4
  • 54
    • 0035963313 scopus 로고    scopus 로고
    • Site-specific and temporally-regulated retinoblastoma protein dephosphorylation by protein phosphatase type 1
    • Rubin, E., Mittnacht, S., Villa-Moruzzi, E., Ludlow, J.W. Site-specific and temporally-regulated retinoblastoma protein dephosphorylation by protein phosphatase type 1. Oncogene 2001, 20: 3776-85.
    • (2001) Oncogene , vol.20 , pp. 3776-3785
    • Rubin, E.1    Mittnacht, S.2    Villa-Moruzzi, E.3    Ludlow, J.W.4
  • 55
    • 0028214026 scopus 로고    scopus 로고
    • Dohadwala, M., da Cruz e Silva, E.F., Hall, F.L. et al. Phosphorylation and inactivation of protein phosphatase 1 by cyclin-dependent kinases. Proc Natl Acad Sci USA 1994, 91: 6408-12.
    • Dohadwala, M., da Cruz e Silva, E.F., Hall, F.L. et al. Phosphorylation and inactivation of protein phosphatase 1 by cyclin-dependent kinases. Proc Natl Acad Sci USA 1994, 91: 6408-12.
  • 56
    • 12644291188 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of mammalian protein phosphatase 1 by cdc2 kinase
    • Kwon, Y.G., Lee, S.Y., Choi, Y., Greengard, P., Nairn, A.C. Cell cycle-dependent phosphorylation of mammalian protein phosphatase 1 by cdc2 kinase. Proc Natl Acad Sci USA 1997, 94: 2168-73.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2168-2173
    • Kwon, Y.G.1    Lee, S.Y.2    Choi, Y.3    Greengard, P.4    Nairn, A.C.5
  • 58
    • 0031172801 scopus 로고    scopus 로고
    • Constitutively active protein phosphatase 1α causes Rb-dependent G1 arrest in human cancer cells
    • Berndt, N., Dohadwala, M., Liu, C.W. Constitutively active protein phosphatase 1α causes Rb-dependent G1 arrest in human cancer cells. Curr Biol 1997, 7: 375-86.
    • (1997) Curr Biol , vol.7 , pp. 375-386
    • Berndt, N.1    Dohadwala, M.2    Liu, C.W.3
  • 59
    • 9644262529 scopus 로고    scopus 로고
    • Fer kinase sustains the activation level of ERK1/2 and increases the production of VEGF in hypoxic cells
    • Salem, Y., Shpungin, S., Pasder, O. et al. Fer kinase sustains the activation level of ERK1/2 and increases the production of VEGF in hypoxic cells. Cell Signal 2005, 17: 341-53.
    • (2005) Cell Signal , vol.17 , pp. 341-353
    • Salem, Y.1    Shpungin, S.2    Pasder, O.3
  • 60
    • 0036010598 scopus 로고    scopus 로고
    • Regulator-driven functional diversification of protein phosphatase-1 in eukaryotic evolution
    • Ceulemans, H., Stalmans, W., Bollen, M. Regulator-driven functional diversification of protein phosphatase-1 in eukaryotic evolution. Bioessays 2002, 24: 371-81.
    • (2002) Bioessays , vol.24 , pp. 371-381
    • Ceulemans, H.1    Stalmans, W.2    Bollen, M.3
  • 61
    • 0346728803 scopus 로고    scopus 로고
    • Functional diversity of protein phosphatase-1, a cellular economizer and reset button
    • Ceulemans, H., Bollen, M. Functional diversity of protein phosphatase-1, a cellular economizer and reset button. Physiol Rev 2004, 84: 1-39.
    • (2004) Physiol Rev , vol.84 , pp. 1-39
    • Ceulemans, H.1    Bollen, M.2
  • 62
    • 0036032778 scopus 로고    scopus 로고
    • Regulators of serine/threonine protein phosphatases at the dawn of a clinical era?
    • Honkanen, R.E., Golden, T. Regulators of serine/threonine protein phosphatases at the dawn of a clinical era? Curr Med Chem 2002, 9: 2055-75.
    • (2002) Curr Med Chem , vol.9 , pp. 2055-2075
    • Honkanen, R.E.1    Golden, T.2
  • 63
    • 0037024344 scopus 로고    scopus 로고
    • A putative nuclear receptor coactivator (TMF/ARA160) associates with hbrm/hSNF2 α and BRG-1/hSNF2 β and localizes in the Golgi apparatus
    • Mori, K., Kato, H. A putative nuclear receptor coactivator (TMF/ARA160) associates with hbrm/hSNF2 α and BRG-1/hSNF2 β and localizes in the Golgi apparatus. FEBS Lett 2002, 520: 127-32.
    • (2002) FEBS Lett , vol.520 , pp. 127-132
    • Mori, K.1    Kato, H.2
  • 64
    • 0033529601 scopus 로고    scopus 로고
    • Isolation and characterization of ARA160 as the first androgen receptor N-terminal-associated coactivator in human prostate cells
    • Hsiao, P.W., Chang, C. Isolation and characterization of ARA160 as the first androgen receptor N-terminal-associated coactivator in human prostate cells. J Biol Chem 1999, 274: 22373-9.
    • (1999) J Biol Chem , vol.274 , pp. 22373-22379
    • Hsiao, P.W.1    Chang, C.2
  • 65
    • 0026701259 scopus 로고
    • Cloning and chromosomal mapping of a human immunodeficiency virus 1 "TATA" element modulatory factor
    • Garcia, J.A., Ou, S.H., Wu, F., Lusis, A.J., Sparkes, R.S., Gaynor, R.B. Cloning and chromosomal mapping of a human immunodeficiency virus 1 "TATA" element modulatory factor. Proc Natl Acad Sci USA 1992, 89: 9372-6.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9372-9376
    • Garcia, J.A.1    Ou, S.H.2    Wu, F.3    Lusis, A.J.4    Sparkes, R.S.5    Gaynor, R.B.6
  • 66
    • 10444236367 scopus 로고    scopus 로고
    • TMF is a golgin that binds Rab6 and influences Golgi morphology
    • Fridmann-Sirkis, Y., Siniossoglou, S., Pelham, H.R. TMF is a golgin that binds Rab6 and influences Golgi morphology. BMC Cell Biol 2004, 5: 18.
    • (2004) BMC Cell Biol , vol.5 , pp. 18
    • Fridmann-Sirkis, Y.1    Siniossoglou, S.2    Pelham, H.R.3
  • 67
    • 0032407062 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the TATA element modulatory factor by the FER nuclear tyrosine kinases
    • Schwartz, Y., Ben-Dor, I., Navon, A., Motro, B., Nir, U. Tyrosine phosphorylation of the TATA element modulatory factor by the FER nuclear tyrosine kinases. FEBS Lett 1998, 434: 339-45.
    • (1998) FEBS Lett , vol.434 , pp. 339-345
    • Schwartz, Y.1    Ben-Dor, I.2    Navon, A.3    Motro, B.4    Nir, U.5
  • 68
    • 10644271682 scopus 로고    scopus 로고
    • TMF/ARA160 is a BC-box-containing protein that mediates the degradation of STAT3
    • Perry, E., Tsruya, R., Levitsky, P. et al. TMF/ARA160 is a BC-box-containing protein that mediates the degradation of STAT3. Oncogene 2004, 23: 8908-19.
    • (2004) Oncogene , vol.23 , pp. 8908-8919
    • Perry, E.1    Tsruya, R.2    Levitsky, P.3
  • 69
    • 0036383262 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor complex and regulation of hypoxia-inducible transcription
    • Conaway, R.C., Conaway, J.W. The von Hippel-Lindau tumor suppressor complex and regulation of hypoxia-inducible transcription. Adv Cancer Res 2002, 85: 1-12.
    • (2002) Adv Cancer Res , vol.85 , pp. 1-12
    • Conaway, R.C.1    Conaway, J.W.2
  • 70
    • 0032540499 scopus 로고    scopus 로고
    • The Elongin BC complex and the von Hippel-Lindau tumor suppressor protein
    • Conaway, J.W., Kamura, T., Conaway, R.C. The Elongin BC complex and the von Hippel-Lindau tumor suppressor protein. Biochim Biophys Acta 1998, 1377: M49-54.
    • (1998) Biochim Biophys Acta , vol.1377
    • Conaway, J.W.1    Kamura, T.2    Conaway, R.C.3
  • 71
    • 0036718539 scopus 로고    scopus 로고
    • Molecular basis of the VHL hereditary cancer syndrome
    • Kaelin, W.G. Jr. Molecular basis of the VHL hereditary cancer syndrome. Nat Rev Cancer 2002, 2: 673-82.
    • (2002) Nat Rev Cancer , vol.2 , pp. 673-682
    • Kaelin Jr., W.G.1
  • 72
    • 0036359548 scopus 로고    scopus 로고
    • Hypoxia - A key regulatory factor in tumour growth
    • Harris, A.L. Hypoxia - A key regulatory factor in tumour growth. Nat Rev Cancer 2002, 2: 38-47.
    • (2002) Nat Rev Cancer , vol.2 , pp. 38-47
    • Harris, A.L.1
  • 73
    • 0036006171 scopus 로고    scopus 로고
    • Vascular endothelial growth factor (VEGF), a survival factor for tumour cells: Implications for anti-angiogenic therapy
    • Harmey, J.H., Bouchier-Hayes, D. Vascular endothelial growth factor (VEGF), a survival factor for tumour cells: Implications for anti-angiogenic therapy. Bioessays 2002, 24: 280-3.
    • (2002) Bioessays , vol.24 , pp. 280-283
    • Harmey, J.H.1    Bouchier-Hayes, D.2
  • 74
    • 0032537757 scopus 로고    scopus 로고
    • Regulation of vascular endothelial growth factor (VEGF) expression is mediated by internal initiation of translation and alternative initiation of transcription
    • Akiri, G., Nahari, D., Finkelstein, Y., Le, S.Y., Elroy-Stein, O., Levi, B.Z. Regulation of vascular endothelial growth factor (VEGF) expression is mediated by internal initiation of translation and alternative initiation of transcription. Oncogene 1998, 17: 227-36.
    • (1998) Oncogene , vol.17 , pp. 227-236
    • Akiri, G.1    Nahari, D.2    Finkelstein, Y.3    Le, S.Y.4    Elroy-Stein, O.5    Levi, B.Z.6
  • 75
    • 0036527906 scopus 로고    scopus 로고
    • Two HIFs may be better than one
    • Seagroves, T., Johnson, R.S. Two HIFs may be better than one. Cancer Cell 2002, 1: 211-3.
    • (2002) Cancer Cell , vol.1 , pp. 211-213
    • Seagroves, T.1    Johnson, R.S.2
  • 76
    • 0242330181 scopus 로고    scopus 로고
    • Oxygen sensing in the hypoxic response pathway: Regulation of the hypoxia-inducible transcription factor
    • Bruick, R.K. Oxygen sensing in the hypoxic response pathway: Regulation of the hypoxia-inducible transcription factor. Genes Dev 2003, 17: 2614-23.
    • (2003) Genes Dev , vol.17 , pp. 2614-2623
    • Bruick, R.K.1
  • 77
    • 3843095197 scopus 로고    scopus 로고
    • HIF-1's relationship to oxygen: Simple yet sophisticated
    • Maxwell, P.H. HIF-1's relationship to oxygen: Simple yet sophisticated. Cell Cycle 2004, 3: 156-9.
    • (2004) Cell Cycle , vol.3 , pp. 156-159
    • Maxwell, P.H.1
  • 78
    • 0032725554 scopus 로고    scopus 로고
    • p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1α (HIF-1α) and enhance the transcriptional activity of HIF-1
    • Richard, D.E., Berra, E., Gothie, E., Roux, D., Pouyssegur, J. p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1α (HIF-1α) and enhance the transcriptional activity of HIF-1. J Biol Chem 1999, 274: 32631-7.
    • (1999) J Biol Chem , vol.274 , pp. 32631-32637
    • Richard, D.E.1    Berra, E.2    Gothie, E.3    Roux, D.4    Pouyssegur, J.5
  • 79
    • 0033981845 scopus 로고    scopus 로고
    • ERK activation upon hypoxia: Involvement in HIF-1 activation
    • Minet, E., Arnould, T., Michel, G. et al. ERK activation upon hypoxia: Involvement in HIF-1 activation. FEBS Lett 2000, 468: 53-8.
    • (2000) FEBS Lett , vol.468 , pp. 53-58
    • Minet, E.1    Arnould, T.2    Michel, G.3
  • 80
    • 0034668187 scopus 로고    scopus 로고
    • Signaling angiogenesis via p42/p44 MAP kinase and hypoxia
    • Berra, E., Milanini, J., Richard, D.E. et al. Signaling angiogenesis via p42/p44 MAP kinase and hypoxia. Biochem Pharmacol 2000, 60: 1171-8.
    • (2000) Biochem Pharmacol , vol.60 , pp. 1171-1178
    • Berra, E.1    Milanini, J.2    Richard, D.E.3
  • 81
    • 10744219591 scopus 로고    scopus 로고
    • Suppression of the dual-specificity phosphatase MKP-1 enhances HIF-1 trans-activation and increases expression of EPO
    • Liu, C., Shi, Y., Han, Z. et al. Suppression of the dual-specificity phosphatase MKP-1 enhances HIF-1 trans-activation and increases expression of EPO. Biochem Biophys Res Commun 2003, 312: 780-6.
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 780-786
    • Liu, C.1    Shi, Y.2    Han, Z.3
  • 82
    • 0033970533 scopus 로고    scopus 로고
    • Dual specificity phosphatases: A gene family for control of MAP kinase function
    • Camps, M., Nichols, A., Arkinstall, S. Dual specificity phosphatases: A gene family for control of MAP kinase function. FASEB J 2000, 14: 6-16.
    • (2000) FASEB J , vol.14 , pp. 6-16
    • Camps, M.1    Nichols, A.2    Arkinstall, S.3
  • 83
    • 0033617186 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase phosphatase-1 (MKP-1) expression is induced by low oxygen conditions found in solid tumor microenvironments. A candidate MKP for the inactivation of hypoxia-inducible stress-activated protein kinase/c-Jun N-terminal protein kinase activity
    • Laderoute, K.R., Mendonca, H.L., Calaoagan, J.M., Knapp, A.M., Giaccia, A.J., Stork, P.J. Mitogen-activated protein kinase phosphatase-1 (MKP-1) expression is induced by low oxygen conditions found in solid tumor microenvironments. A candidate MKP for the inactivation of hypoxia-inducible stress-activated protein kinase/c-Jun N-terminal protein kinase activity. J Biol Chem 1999, 274: 12890-7.
    • (1999) J Biol Chem , vol.274 , pp. 12890-12897
    • Laderoute, K.R.1    Mendonca, H.L.2    Calaoagan, J.M.3    Knapp, A.M.4    Giaccia, A.J.5    Stork, P.J.6
  • 84
    • 0037131170 scopus 로고    scopus 로고
    • Brain genomic response following hypoxia and re-oxygenation in the neonatal rat. Identification of genes that might contribute to hypoxia-induced ischemic tolerance
    • Bernaudin, M., Tang, Y., Reilly, M., Petit, E., Sharp, F.R. Brain genomic response following hypoxia and re-oxygenation in the neonatal rat. Identification of genes that might contribute to hypoxia-induced ischemic tolerance. J Biol Chem 2002, 277: 39728-38.
    • (2002) J Biol Chem , vol.277 , pp. 39728-39738
    • Bernaudin, M.1    Tang, Y.2    Reilly, M.3    Petit, E.4    Sharp, F.R.5
  • 85
    • 0035977013 scopus 로고    scopus 로고
    • Hypoxia-induced regulation of MAPK phosphatase-1 as identified by subtractive suppression hybridization and cDNA microarray analysis
    • Seta, K.A., Kim, R., Kim, H.W., Millhorn, D.E., Beitner-Johnson, D. Hypoxia-induced regulation of MAPK phosphatase-1 as identified by subtractive suppression hybridization and cDNA microarray analysis. J Biol Chem 2001, 276: 44405-12.
    • (2001) J Biol Chem , vol.276 , pp. 44405-44412
    • Seta, K.A.1    Kim, R.2    Kim, H.W.3    Millhorn, D.E.4    Beitner-Johnson, D.5
  • 86
    • 21444435325 scopus 로고    scopus 로고
    • Abl-kinase-sensitive levels of ERK5 and its intrinsic basal activity contribute to leukaemia cell survival
    • Buschbeck, M., Hofbauer, S., Di Croce, L., Keri, G., Ullrich, A. Abl-kinase-sensitive levels of ERK5 and its intrinsic basal activity contribute to leukaemia cell survival. EMBO Rep 2005, 6: 63-9.
    • (2005) EMBO Rep , vol.6 , pp. 63-69
    • Buschbeck, M.1    Hofbauer, S.2    Di Croce, L.3    Keri, G.4    Ullrich, A.5
  • 87
    • 0034634581 scopus 로고    scopus 로고
    • Requirement of cyclin/Cdk2 and protein phosphatase 1 activity for chromatin assembly factor 1-dependent chromatin assembly during DNA synthesis
    • Keller, C., Krude, T. Requirement of cyclin/Cdk2 and protein phosphatase 1 activity for chromatin assembly factor 1-dependent chromatin assembly during DNA synthesis. J Biol Chem 2000, 275: 35512-21.
    • (2000) J Biol Chem , vol.275 , pp. 35512-35521
    • Keller, C.1    Krude, T.2
  • 88
    • 0642347848 scopus 로고    scopus 로고
    • Roles and regulation of serine/threonine-specific protein phosphatases in the cell cycle
    • Berndt, N. Roles and regulation of serine/threonine-specific protein phosphatases in the cell cycle. Prog Cell Cycle Res 2003, 5: 497-510.
    • (2003) Prog Cell Cycle Res , vol.5 , pp. 497-510
    • Berndt, N.1


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