메뉴 건너뛰기




Volumn 6, Issue 4, 2006, Pages 321-330

Targeting polo-like kinase 1 for cancer therapy

Author keywords

[No Author keywords available]

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; ANTINEOPLASTIC AGENT; BI 2536; ENZYME INHIBITOR; HESPERADIN; MORIN; N [4 [6 METHOXY 7 (3 MORPHOLINOPROPOXY) 4 QUINAZOLINYLAMINO]PHENYL] BENZAMIDE; N [4 [6 METHOXY 7 (3 MORPHOLINOPROPOXY) 4 QUINAZOLINYLAMINO]PHENYL]BENZAMIDE; ON 01910; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; PHOSPHOTRANSFERASE INHIBITOR; POLO LIKE KINASE 1; QUERCETIN; SCYTONEMIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; VX 680; WORTMANNIN;

EID: 33645316142     PISSN: 1474175X     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrc1841     Document Type: Review
Times cited : (750)

References (129)
  • 1
    • 0027280212 scopus 로고
    • A conserved mitotic kinase active at late anaphase-telophase in syncytial Drosophila embryos
    • Fenton, B. & Glover, D. M. A conserved mitotic kinase active at late anaphase-telophase in syncytial Drosophila embryos. Nature 363, 637-640 (1993).
    • (1993) Nature , vol.363 , pp. 637-640
    • Fenton, B.1    Glover, D.M.2
  • 2
    • 0032535244 scopus 로고    scopus 로고
    • Polo-like kinases: A team that plays throughout mitosis
    • Glover, D. M., Hagan, I. M. & Tavares, A. A. Polo-like kinases: a team that plays throughout mitosis. Genes Dev. 12, 3777-3787 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 3777-3787
    • Glover, D.M.1    Hagan, I.M.2    Tavares, A.A.3
  • 3
    • 0027178446 scopus 로고
    • Identification and cloning of a protein kinase-encoding mouse gene, Plk, related to the polo gene of Drosophila
    • Clay, F. J., McEwen, S. J., Bertoncello, I., Wilks, A. F. & Dunn, A. R. Identification and cloning of a protein kinase-encoding mouse gene, Plk, related to the polo gene of Drosophila. Proc. Natl Acad. Sci. USA 90, 4882-4886 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4882-4886
    • Clay, F.J.1    McEwen, S.J.2    Bertoncello, I.3    Wilks, A.F.4    Dunn, A.R.5
  • 4
    • 0027524588 scopus 로고
    • Cell cycle-and terminal differentiation-associated regulation of the mouse mRNA encoding a conserved mitotic protein kinase
    • Lake, R. J. & Jelinek, W. R. Cell cycle-and terminal differentiation-associated regulation of the mouse mRNA encoding a conserved mitotic protein kinase. Mol. Cell. Biol. 13, 7793-7801 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7793-7801
    • Lake, R.J.1    Jelinek, W.R.2
  • 5
    • 0028348704 scopus 로고
    • Induction and down-regulation of PLK, a human serine/threonine kinase expressed in proliferating cells and tumors
    • Holtrich, U. et al. Induction and down-regulation of PLK, a human serine/threonine kinase expressed in proliferating cells and tumors. Proc. Natl Acad. Sci. USA 91, 1736-1740 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1736-1740
    • Holtrich, U.1
  • 6
    • 0027977923 scopus 로고
    • Cloning and characterization of human and murine homologues of the Drosophila polo serine-threonine kinase
    • Hamanaka, R. et al. Cloning and characterization of human and murine homologues of the Drosophila polo serine-threonine kinase. Cell Growth Differ. 5, 249-257 (1994).
    • (1994) Cell Growth Differ. , vol.5 , pp. 249-257
    • Hamanaka, R.1
  • 7
    • 0026665462 scopus 로고
    • Identification of an early-growth-response gene encoding a novel putative protein kinase
    • Simmons, D. L., Neel, B. G., Stevens, R., Evett, G. & Erikson, R. L. Identification of an early-growth-response gene encoding a novel putative protein kinase. Mol. Cell. Biol. 12, 4164-4169 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4164-4169
    • Simmons, D.L.1    Neel, B.G.2    Stevens, R.3    Evett, G.4    Erikson, R.L.5
  • 8
    • 0030695943 scopus 로고    scopus 로고
    • Human Prk is a conserved protein serine/threonine kinase involved in regulating M phase functions
    • Ouyang, B. et al. Human Prk is a conserved protein serine/threonine kinase involved in regulating M phase functions. J. Biol. Chem. 272, 28646-28651 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 28646-28651
    • Ouyang, B.1
  • 9
    • 0034609729 scopus 로고    scopus 로고
    • Adhesion induced expression of the serine/threonine kinase Fnk in human macrophages
    • Holtrich, U. et al. Adhesion induced expression of the serine/threonine kinase Fnk in human macrophages. Oncogene 19, 4832-4839 (2000).
    • (2000) Oncogene , vol.19 , pp. 4832-4839
    • Holtrich, U.1
  • 10
    • 0028336680 scopus 로고
    • Sak, a murine protein-serine/threonine kinase that is related to the Drosophila polo kinase and involved in cell proliferation
    • Fode, C., Motro, B., Yousefi, S., Heffernan, M. & Dennis, J. W. Sak, a murine protein-serine/threonine kinase that is related to the Drosophila polo kinase and involved in cell proliferation. Proc. Natl Acad. Sci. USA 91, 6388-6392 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6388-6392
    • Fode, C.1    Motro, B.2    Yousefi, S.3    Heffernan, M.4    Dennis, J.W.5
  • 11
    • 0030954076 scopus 로고    scopus 로고
    • Human SAK related to the PLK/polo family of cell cycle kinases shows high mRNA expression in testis
    • Karn, T. et al. Human SAK related to the PLK/polo family of cell cycle kinases shows high mRNA expression in testis. Oncol. Reports 4, 505-510 (1997).
    • (1997) Oncol. Reports , vol.4 , pp. 505-510
    • Karn, T.1
  • 12
    • 0031581099 scopus 로고    scopus 로고
    • On the regulation and function of human polo-like kinase 1 (PLK1): Effects of overexpression on cell cycle progression
    • Mundt, K. E., Golsteyn, R. M., Lane, H. A. & Nigg, E. A. On the regulation and function of human polo-like kinase 1 (PLK1): effects of overexpression on cell cycle progression. Biochem. Biophys. Res. Commun. 239, 377-385 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 377-385
    • Mundt, K.E.1    Golsteyn, R.M.2    Lane, H.A.3    Nigg, E.A.4
  • 13
    • 0031578244 scopus 로고    scopus 로고
    • Malignant transformation of mammalian cells initiated by constitutive expression of the polo-like kinase
    • Smith, M. R. et al. Malignant transformation of mammalian cells initiated by constitutive expression of the polo-like kinase. Biochem. Biophys. Res. Commun. 234, 397-405 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 397-405
    • Smith, M.R.1
  • 14
    • 13244269808 scopus 로고    scopus 로고
    • Polo-like kinases and oncogenesis
    • Eckerdt, F., Yuan, J. & Strebhardt, K. Polo-like kinases and oncogenesis. Oncogene 24, 267-276 (2005).
    • (2005) Oncogene , vol.24 , pp. 267-276
    • Eckerdt, F.1    Yuan, J.2    Strebhardt, K.3
  • 15
    • 0036185931 scopus 로고    scopus 로고
    • Scytonemin-a marine natural product inhibitor of kinases key in hyperproliferative inflammatory diseases
    • Stevenson, C. S. et al. Scytonemin-a marine natural product inhibitor of kinases key in hyperproliferative inflammatory diseases. Inflamm. Res. 51, 112-114 (2002).
    • (2002) Inflamm. Res. , vol.51 , pp. 112-114
    • Stevenson, C.S.1
  • 16
    • 0036827627 scopus 로고    scopus 로고
    • The identification and characterization of the marine natural product scytonemin as a novel antiproliferative pharmacophore
    • Stevenson, C. S. et al. The identification and characterization of the marine natural product scytonemin as a novel antiproliferative pharmacophore. J. Pharmacol. Exp. Ther. 303, 858-866 (2002).
    • (2002) J. Pharmacol. Exp. Ther. , vol.303 , pp. 858-866
    • Stevenson, C.S.1
  • 17
    • 12344256951 scopus 로고    scopus 로고
    • Wortmannin, a widely used phosphoinositide 3-kinase inhibitor, also potently inhibits mammalian polo-like kinase
    • Liu, Y. et al. Wortmannin, a widely used phosphoinositide 3-kinase inhibitor, also potently inhibits mammalian polo-like kinase. Chem. Biol. 12, 99-107 (2005).
    • (2005) Chem. Biol. , vol.12 , pp. 99-107
    • Liu, Y.1
  • 18
    • 33645323416 scopus 로고    scopus 로고
    • BI 2536, a potent and highly selective inhibitor of Polo-like kinase 1 (Plk1), induces mitotic arrest and apoptosis in a broad spectrum of tumor cell lines
    • Steegmaier, M. et al. BI 2536, a potent and highly selective inhibitor of Polo-like kinase 1 (Plk1), induces mitotic arrest and apoptosis in a broad spectrum of tumor cell lines. Clin. Cancer Res. 11 (Suppl.), 9147 (2005).
    • (2005) Clin. Cancer Res. , vol.11 , Issue.SUPPL. , pp. 9147
    • Steegmaier, M.1
  • 19
    • 33645280803 scopus 로고    scopus 로고
    • In vivo activity of BI 2536, a potent and selective inhibitor of the mitotic kinase Plk1, in a range of human cancer xenograft models
    • Baum A et al. In vivo activity of BI 2536, a potent and selective inhibitor of the mitotic kinase Plk1, in a range of human cancer xenograft models. Clin. Cancer Res. 11 (Suppl.), 9146 (2005).
    • (2005) Clin. Cancer Res. , vol.11 , Issue.SUPPL. , pp. 9146
    • Baum, A.1
  • 20
    • 33645287475 scopus 로고    scopus 로고
    • A phase I single dose escalation study of the Polo-like kinase 1 (Plk1) inhibitor BI 2536 in patients with advanced solid tumors
    • Mross K et al. A phase I single dose escalation study of the Polo-like kinase 1 (Plk1) inhibitor BI 2536 in patients with advanced solid tumors. Clin. Cancer Res. 11 (Suppl.), 9032 (2005).
    • (2005) Clin. Cancer Res. , vol.11 , Issue.SUPPL. , pp. 9032
    • Mross, K.1
  • 21
    • 17644368237 scopus 로고    scopus 로고
    • ON01910, a non-ATP-competitive small molecule inhibitor of Plk1, is a potent anticancer agent
    • Gumireddy, K. et al. ON01910, a non-ATP-competitive small molecule inhibitor of Plk1, is a potent anticancer agent. Cancer Cell 7, 275-286 (2005).
    • (2005) Cancer Cell , vol.7 , pp. 275-286
    • Gumireddy, K.1
  • 22
    • 2942615282 scopus 로고    scopus 로고
    • Polo-like kinases and the orchestration of cell division
    • Barr, F. A., Sillje, H. H. & Nigg, E. A. Polo-like kinases and the orchestration of cell division. Nature Rev. Mol. Cell Biol. 5, 429-440 (2004).
    • (2004) Nature Rev. Mol. Cell Biol. , vol.5 , pp. 429-440
    • Barr, F.A.1    Sillje, H.H.2    Nigg, E.A.3
  • 23
    • 13244258316 scopus 로고    scopus 로고
    • Regulation of cell cycle checkpoints by polo-like kinases
    • Xie, S., Xie, B., Lee, M. Y. & Dai, W. Regulation of cell cycle checkpoints by polo-like kinases. Oncogene 24, 277-286 (2005).
    • (2005) Oncogene , vol.24 , pp. 277-286
    • Xie, S.1    Xie, B.2    Lee, M.Y.3    Dai, W.4
  • 24
    • 18344366048 scopus 로고    scopus 로고
    • Getting in and out of mitosis with Polo-like kinase-1
    • van Vugt, M. A. & Medema, R. H. Getting in and out of mitosis with Polo-like kinase-1. Oncogene 24, 2844-2859 (2005).
    • (2005) Oncogene , vol.24 , pp. 2844-2859
    • Van Vugt, M.A.1    Medema, R.H.2
  • 25
    • 0028243084 scopus 로고
    • Cell cycle analysis and chromosomal localization of human Plk1, a putative homologue of the mitotic kinases Drosophila polo and Saccharomyces cerevisiae Cdc5
    • Golsteyn, R. M. et al. Cell cycle analysis and chromosomal localization of human Plk1, a putative homologue of the mitotic kinases Drosophila polo and Saccharomyces cerevisiae Cdc5. J. Cell Sci. 107, 1509-1517 (1994).
    • (1994) J. Cell Sci. , vol.107 , pp. 1509-1517
    • Golsteyn, R.M.1
  • 26
    • 0029079267 scopus 로고
    • Cell cycle regulation of the activity and subcellular localization of Plk1, a human protein kinase implicated in mitotic spindle function
    • Golsteyn, R. M., Mundt, K. E., Fry, A. M. & Nigg, E. A. Cell cycle regulation of the activity and subcellular localization of Plk1, a human protein kinase implicated in mitotic spindle function. J. Cell Biol. 129, 1617-1628 (1995).
    • (1995) J. Cell Biol. , vol.129 , pp. 1617-1628
    • Golsteyn, R.M.1    Mundt, K.E.2    Fry, A.M.3    Nigg, E.A.4
  • 27
    • 0028884602 scopus 로고
    • Plk is an M-phase-specific protein kinase and interacts with a kinesin-like protein, CHO1/MKLP-1
    • Lee, K. S., Yuan, Y. L., Kuriyama, R. & Erikson, R. L. Plk is an M-phase-specific protein kinase and interacts with a kinesin-like protein, CHO1/MKLP-1. Mol. Cell. Biol. 15, 7143-7151 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 7143-7151
    • Lee, K.S.1    Yuan, Y.L.2    Kuriyama, R.3    Erikson, R.L.4
  • 28
    • 0023804548 scopus 로고
    • Polo, a mitotic mutant of Drosophila displaying abnormal spindle poles
    • Sunkel, C. E. & Glover, D. M. polo, a mitotic mutant of Drosophila displaying abnormal spindle poles. J. Cell Sci. 89, 25-38 (1988).
    • (1988) J. Cell Sci. , vol.89 , pp. 25-38
    • Sunkel, C.E.1    Glover, D.M.2
  • 29
    • 0027173110 scopus 로고
    • A multicopy suppressor gene of the Saccharomyces cerevisiae G1 cell cycle mutant gene dbf4 encodes a protein kinase and is identified as CDC5
    • Kitada, K., Johnson, A. L., Johnston, L. H. & Sugino, A. A multicopy suppressor gene of the Saccharomyces cerevisiae G1 cell cycle mutant gene dbf4 encodes a protein kinase and is identified as CDC5. Mol. Cell. Biol. 13, 4445-4457 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4445-4457
    • Kitada, K.1    Johnson, A.L.2    Johnston, L.H.3    Sugino, A.4
  • 30
    • 0029008281 scopus 로고
    • The conserved Schizosaccharomyces pombe kinase plo1, required to form a bipolar spindle, the actin ring, and septum, can drive septum formation in G1 and G2 cells
    • Ohkura, H., Hagan, I. M. & Glover, D. M. The conserved Schizosaccharomyces pombe kinase plo1, required to form a bipolar spindle, the actin ring, and septum, can drive septum formation in G1 and G2 cells. Genes Dev. 9, 1059-1073 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 1059-1073
    • Ohkura, H.1    Hagan, I.M.2    Glover, D.M.3
  • 31
    • 0032415593 scopus 로고    scopus 로고
    • GFP tagging reveals human Polo-like kinase 1 at the kinetochore/ centromere region of mitotic chromosomes
    • Arnaud, L., Pines, J. & Nigg, E. A. GFP tagging reveals human Polo-like kinase 1 at the kinetochore/centromere region of mitotic chromosomes. Chromosoma 107, 424-429 (1998).
    • (1998) Chromosoma , vol.107 , pp. 424-429
    • Arnaud, L.1    Pines, J.2    Nigg, E.A.3
  • 32
    • 0032441303 scopus 로고    scopus 로고
    • Mouse polo-like kinase 1 associates with the acentriolar spindle poles, meiotic chromosomes and spindle midzone during oocyte maturation
    • Wianny, F., Tavares, A., Evans, M. J., Glover, D. M. & Zernicka-Goetz, M. Mouse polo-like kinase 1 associates with the acentriolar spindle poles, meiotic chromosomes and spindle midzone during oocyte maturation. Chromosoma 107, 430-439 (1998).
    • (1998) Chromosoma , vol.107 , pp. 430-439
    • Wianny, F.1    Tavares, A.2    Evans, M.J.3    Glover, D.M.4    Zernicka-Goetz, M.5
  • 33
    • 0030924977 scopus 로고    scopus 로고
    • Plk is a functional homolog of Saccharomyces cerevisiae Cdc5, and elevated Plk activity induces multiple septation structures
    • Lee, K. S. & Erikson, R. L. Plk is a functional homolog of Saccharomyces cerevisiae Cdc5, and elevated Plk activity induces multiple septation structures. Mol. Cell. Biol. 17, 3408-3417 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3408-3417
    • Lee, K.S.1    Erikson, R.L.2
  • 34
    • 0037172998 scopus 로고    scopus 로고
    • Activation of Cdc2/cyclin B and inhibition of centrosome amplification in cells depleted of Plk1 by siRNA
    • Liu, X. & Erikson, R. L. Activation of Cdc2/cyclin B and inhibition of centrosome amplification in cells depleted of Plk1 by siRNA. Proc. Natl Acad. Sci. USA 99, 8672-8676 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 8672-8676
    • Liu, X.1    Erikson, R.L.2
  • 35
    • 0038624074 scopus 로고    scopus 로고
    • Polo-like kinase (Plk)1 depletion induces apoptosis in cancer cells
    • Liu, X. & Erikson, R. L. Polo-like kinase (Plk)1 depletion induces apoptosis in cancer cells. Proc. Natl Acad. Sci. USA 100, 5789-5794 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5789-5794
    • Liu, X.1    Erikson, R.L.2
  • 36
    • 0037133203 scopus 로고    scopus 로고
    • Functional studies on the role of the C-terminal domain of mammalian polo-like kinase
    • Jang, Y. J., Lin, C. Y., Ma, S. & Erikson, R. L. Functional studies on the role of the C-terminal domain of mammalian polo-like kinase. Proc. Natl Acad. Sci. USA 99, 1984-1989 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 1984-1989
    • Jang, Y.J.1    Lin, C.Y.2    Ma, S.3    Erikson, R.L.4
  • 37
    • 0034282252 scopus 로고    scopus 로고
    • Polo-like kinase-1 is a target of the DNA damage checkpoint
    • Smits, V. A. et al. Polo-like kinase-1 is a target of the DNA damage checkpoint. Nature Cell Biol. 2, 672-676 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 672-676
    • Smits, V.A.1
  • 38
    • 4444321565 scopus 로고    scopus 로고
    • Polo-like kinase-1 controls recovery from a G2 DNA damage-induced arrest in mammalian cells
    • van Vugt, M. A., Bras, A. & Medema, R. H. Polo-like kinase-1 controls recovery from a G2 DNA damage-induced arrest in mammalian cells. Mol. Cell 15, 799-811 (2004).
    • (2004) Mol. Cell , vol.15 , pp. 799-811
    • Van Vugt, M.A.1    Bras, A.2    Medema, R.H.3
  • 39
    • 23844494690 scopus 로고    scopus 로고
    • Restarting the cell cycle when the checkpoint comes to a halt
    • van Vugt, M. A., Bras, A. & Medema, R. H. Restarting the cell cycle when the checkpoint comes to a halt. Cancer Res. 65, 7037-7040 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 7037-7040
    • Van Vugt, M.A.1    Bras, A.2    Medema, R.H.3
  • 40
    • 2942623616 scopus 로고    scopus 로고
    • Polo-like kinase 1 (Plk1) inhibits p53 function by physical interaction and phosphorylation
    • Ando, K. et al. Polo-like kinase 1 (Plk1) inhibits p53 function by physical interaction and phosphorylation. J. Biol. Chem. 279, 25549-25561 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 25549-25561
    • Ando, K.1
  • 41
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks, S. K., Quinn, A. M. & Hunter, T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241, 42-52 (1988).
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 42
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members
    • Hanks, S. K. & Quinn, A. M. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol. 200, 38-62 (1991).
    • (1991) Methods Enzymol. , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 43
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. & Peitsch, M. C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (1997).
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 44
    • 0242330123 scopus 로고    scopus 로고
    • Structural basis of Aurora-A activation by TPX2 at the mitotic spindle
    • Bayliss, R., Sardon, T., Vernos, I. & Conti, E. Structural basis of Aurora-A activation by TPX2 at the mitotic spindle. Mol. Cell 12, 851-862 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 851-862
    • Bayliss, R.1    Sardon, T.2    Vernos, I.3    Conti, E.4
  • 45
    • 1842848073 scopus 로고    scopus 로고
    • Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography
    • Nowakowski, J. et al. Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography. Structure. (Camb.) 10, 1659-1667 (2002).
    • (2002) Structure. (Camb.) , vol.10 , pp. 1659-1667
    • Nowakowski, J.1
  • 46
    • 0037044846 scopus 로고    scopus 로고
    • Crystal structure of aurora-2, an oncogenic serine/threonine kinase
    • Cheetham, G. M. et al. Crystal structure of aurora-2, an oncogenic serine/threonine kinase. J. Biol. Chem. 277, 42419-42422 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 42419-42422
    • Cheetham, G.M.1
  • 47
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt/& protein kinase B ternary complex with GSK3-peptide and AMP-PNP
    • Yang, J. et al. Crystal structure of an activated Akt/& protein kinase B ternary complex with GSK3-peptide and AMP-PNP. Nature Struct. Biol. 9, 940-944 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 940-944
    • Yang, J.1
  • 48
    • 13244284602 scopus 로고    scopus 로고
    • Structure and function of Polo-like kinases
    • Lowery, D. M., Lim, D. & Yaffe, M. B. Structure and function of Polo-like kinases. Oncogene 24, 248-259 (2005).
    • (2005) Oncogene , vol.24 , pp. 248-259
    • Lowery, D.M.1    Lim, D.2    Yaffe, M.B.3
  • 49
    • 0029134127 scopus 로고
    • Polo-like kinase is a cell cycle-& regulated kinase activated during mitosis
    • Hamanaka, R. et al. Polo-like kinase is a cell cycle-& regulated kinase activated during mitosis. J. Biol. Chem. 270, 21086-21091 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 21086-21091
    • Hamanaka, R.1
  • 50
    • 0028779479 scopus 로고
    • Signal transduction. Hot lips and phosphorylation of protein kinases
    • Marshall, C. J. Signal transduction. Hot lips and phosphorylation of protein kinases. Nature 367, 686 (1994).
    • (1994) Nature , vol.367 , pp. 686
    • Marshall, C.J.1
  • 51
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D. R. et al. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 414-420 (1991).
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1
  • 52
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D. R. et al. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-414 (1991).
    • (1991) Science , vol.253 , pp. 407-414
    • Knighton, D.R.1
  • 53
    • 0033948542 scopus 로고    scopus 로고
    • Ste20-like kinase (SLK), a regulatory kinase for polo-like kinase (Plk) during the G2/M transition in somatic cells
    • Ellinger-Ziegelbauer, H. et al. Ste20-like kinase (SLK), a regulatory kinase for polo-like kinase (Plk) during the G2/M transition in somatic cells. Genes Cells 5, 491-498 (2000).
    • (2000) Genes Cells , vol.5 , pp. 491-498
    • Ellinger-Ziegelbauer, H.1
  • 54
    • 0038381428 scopus 로고    scopus 로고
    • Stk10, a new member of the polo-like kinase kinase family highly expressed in hematopoietic tissue
    • Walter, S. A., Cutler, R. E. Jr, Martinez, R., Gishizky, M. & Hill, R. J. Stk10, a new member of the polo-like kinase kinase family highly expressed in hematopoietic tissue. J. Biol. Chem. 278, 18221-18228 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 18221-18228
    • Walter, S.A.1    Cutler Jr., R.E.2    Martinez, R.3    Gishizky, M.4    Hill, R.J.5
  • 55
    • 0037067758 scopus 로고    scopus 로고
    • Cell cycle-regulated phosphorylation of the Xenopus polo-& like kinase Plx1
    • Kelm, O., Wind, M., Lehmann, W. D. & Nigg, E. A. Cell cycle-regulated phosphorylation of the Xenopus polo-& like kinase Plx1. J. Biol. Chem. 277, 25247-25256 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 25247-25256
    • Kelm, O.1    Wind, M.2    Lehmann, W.D.3    Nigg, E.A.4
  • 56
    • 10744221449 scopus 로고    scopus 로고
    • The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain
    • Elia, A. E. et al. The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain. Cell 115, 83-95 (2003).
    • (2003) Cell , vol.115 , pp. 83-95
    • Elia, A.E.1
  • 57
    • 0242556820 scopus 로고    scopus 로고
    • The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex
    • Cheng, K. Y., Lowe, E. D., Sinclair, J., Nigg, E. A. & Johnson, L. N. The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex. EMBO J. 22, 5757-5768 (2003).
    • (2003) EMBO J. , vol.22 , pp. 5757-5768
    • Cheng, K.Y.1    Lowe, E.D.2    Sinclair, J.3    Nigg, E.A.4    Johnson, L.N.5
  • 58
    • 0033741651 scopus 로고    scopus 로고
    • Mapping specificity determinants for protein-protein association using protein fusions and random peptide libraries
    • Yaffe, M. B. & Cantley, L. C. Mapping specificity determinants for protein-protein association using protein fusions and random peptide libraries. Methods Enzymol. 328, 157-170 (2000).
    • (2000) Methods Enzymol. , vol.328 , pp. 157-170
    • Yaffe, M.B.1    Cantley, L.C.2
  • 59
    • 0242515843 scopus 로고    scopus 로고
    • Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates
    • Elia, A. E., Cantley, L. C. & Yaffe, M. B. Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates. Science 299, 1228-1231 (2003).
    • (2003) Science , vol.299 , pp. 1228-1231
    • Elia, A.E.1    Cantley, L.C.2    Yaffe, M.B.3
  • 60
    • 0032482986 scopus 로고    scopus 로고
    • Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk
    • Lee, K. S., Grenfell, T. Z., Yarm, F. R. & Erikson, R. L. Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk. Proc. Natl Acad. Sci. USA 95, 9301-9306 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9301-9306
    • Lee, K.S.1    Grenfell, T.Z.2    Yarm, F.R.3    Erikson, R.L.4
  • 61
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson, T. & Nash, P. Assembly of cell regulatory systems through protein interaction domains. Science 300, 445-452 (2003).
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 62
    • 0033740931 scopus 로고    scopus 로고
    • Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2
    • Lin, C. Y. et al. Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2. Proc. Natl Acad. Sci. USA 97, 12589-12594 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 12589-12594
    • Lin, C.Y.1
  • 63
    • 0036334279 scopus 로고    scopus 로고
    • Plk phosphorylation regulates the microtubule-stabilizing protein TCTP
    • Yarm, F. R. Plk phosphorylation regulates the microtubule-stabilizing protein TCTP. Mol. Cell. Biol. 22, 6209-6221 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6209-6221
    • Yarm, F.R.1
  • 64
    • 15444380728 scopus 로고    scopus 로고
    • Plk1 docking to GRASP65 phosphorylated by Cdk1 suggests a mechanism for Golgi checkpoint signalling
    • Preisinger, C. et al. Plk1 docking to GRASP65 phosphorylated by Cdk1 suggests a mechanism for Golgi checkpoint signalling. EMBO J. 24, 753-765 (2005).
    • (2005) EMBO J. , vol.24 , pp. 753-765
    • Preisinger, C.1
  • 65
    • 0033429459 scopus 로고    scopus 로고
    • The polo-box-dependent induction of ectopic septal structures by a mammalian polo kinase, plk, in Saccharomyces cerevisiae
    • Lee, K. S., Song, S. & Erikson, R. L. The polo-box-dependent induction of ectopic septal structures by a mammalian polo kinase, plk, in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 96, 14360-14365 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 14360-14365
    • Lee, K.S.1    Song, S.2    Erikson, R.L.3
  • 66
    • 0037200029 scopus 로고    scopus 로고
    • A spindle checkpoint arrest and a cytokinesis failure by the dominant-negative polo-box domain of Plk1 in U-2 OS cells
    • Seong, Y. S. et al. A spindle checkpoint arrest and a cytokinesis failure by the dominant-negative polo-box domain of Plk1 in U-2 OS cells. J. Biol. Chem. 277, 32282-32293 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 32282-32293
    • Seong, Y.S.1
  • 67
    • 1842372659 scopus 로고    scopus 로고
    • Polo-like kinase, a novel marker for cellular proliferation
    • Yuan, J. et al. Polo-like kinase, a novel marker for cellular proliferation. Am. J. Pathol. 150, 1165-1172 (1997).
    • (1997) Am. J. Pathol. , vol.150 , pp. 1165-1172
    • Yuan, J.1
  • 68
    • 0031051218 scopus 로고    scopus 로고
    • Prognostic significance of polo-like kinase (PLK) expression in non-small cell lung cancer
    • Wolf, G. et al. Prognostic significance of polo-like kinase (PLK) expression in non-small cell lung cancer. Oncogene 14, 543-549 (1997).
    • (1997) Oncogene , vol.14 , pp. 543-549
    • Wolf, G.1
  • 69
    • 0033564832 scopus 로고    scopus 로고
    • Prognostic significance of polo-like kinase (PLK) expression in squamous cell carcinomas of the head and neck
    • Knecht, R. et al. Prognostic significance of polo-like kinase (PLK) expression in squamous cell carcinomas of the head and neck. Cancer Res. 59, 2794-2797 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 2794-2797
    • Knecht, R.1
  • 70
    • 0034693687 scopus 로고    scopus 로고
    • PLK (polo-like kinase), a new prognostic marker for oropharyngeal carcinomas
    • Knecht, R., Oberhauser, C. & Strebhardt, K. PLK (polo-like kinase), a new prognostic marker for oropharyngeal carcinomas. Int. J. Cancer 89, 535-536 (2000).
    • (2000) Int. J. Cancer , vol.89 , pp. 535-536
    • Knecht, R.1    Oberhauser, C.2    Strebhardt, K.3
  • 71
    • 0034716315 scopus 로고    scopus 로고
    • Prognostic value of pololike kinase expression in melanomas
    • Strebhardt, K., Kneisel, L., Linhart, C., Bernd, A. & Kaufmann, R. Prognostic value of pololike kinase expression in melanomas. JAMA 283, 479-480 (2000).
    • (2000) JAMA , vol.283 , pp. 479-480
    • Strebhardt, K.1    Kneisel, L.2    Linhart, C.3    Bernd, A.4    Kaufmann, R.5
  • 72
    • 0035990398 scopus 로고    scopus 로고
    • Expression of polo-like kinase (PLK1) in thin melanomas: A novel marker of metastatic disease
    • Kneisel, L. et al. Expression of polo-like kinase (PLK1) in thin melanomas: a novel marker of metastatic disease. J. Cutan. Pathol. 29, 354-358 (2002).
    • (2002) J. Cutan. Pathol. , vol.29 , pp. 354-358
    • Kneisel, L.1
  • 73
    • 0037648703 scopus 로고    scopus 로고
    • Polo-like kinase 1 (PLK1) is overexpressed in primary colorectal cancers
    • Takahashi, T. et al. Polo-like kinase 1 (PLK1) is overexpressed in primary colorectal cancers. Cancer Sci. 94, 148-152 (2003).
    • (2003) Cancer Sci. , vol.94 , pp. 148-152
    • Takahashi, T.1
  • 74
    • 0034785447 scopus 로고    scopus 로고
    • Comparative expression of the mitotic regulators SAK and PLK in colorectal cancer
    • Macmillan, J. C., Hudson, J. W., Bull, S., Dennis, J. W. & Swallow, C. J. Comparative expression of the mitotic regulators SAK and PLK in colorectal cancer. Ann. Surg. Oncol. 8, 729-740 (2001).
    • (2001) Ann. Surg. Oncol. , vol.8 , pp. 729-740
    • Macmillan, J.C.1    Hudson, J.W.2    Bull, S.3    Dennis, J.W.4    Swallow, C.J.5
  • 75
    • 28044444535 scopus 로고    scopus 로고
    • Polo-like kinase 1 expression is a prognostic factor in human colon cancer
    • Weichert, W. et al. Polo-like kinase 1 expression is a prognostic factor in human colon cancer. World J. Gastroenterol. 11, 5644-5650 (2005).
    • (2005) World J. Gastroenterol. , vol.11 , pp. 5644-5650
    • Weichert, W.1
  • 76
    • 4043092201 scopus 로고    scopus 로고
    • Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: Identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas
    • Yamada, S. et al. Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene 23, 5901-5911 (2004).
    • (2004) Oncogene , vol.23 , pp. 5901-5911
    • Yamada, S.1
  • 77
    • 0037065573 scopus 로고    scopus 로고
    • Identification of high risk breast-cancer patients by gene expression profiling
    • Ahr, A. et al. Identification of high risk breast-cancer patients by gene expression profiling. Lancet 359, 131-132 (2002).
    • (2002) Lancet , vol.359 , pp. 131-132
    • Ahr, A.1
  • 78
    • 0033778278 scopus 로고    scopus 로고
    • Mutations in the Plk gene lead to instability of Plk protein in human tumour cell lines
    • Simizu, S. & Osada, H. Mutations in the Plk gene lead to instability of Plk protein in human tumour cell lines. Nature Cell Biol. 2, 852-854 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 852-854
    • Simizu, S.1    Osada, H.2
  • 79
    • 0025840258 scopus 로고
    • Polo encodes a protein kinase homolog required for mitosis in Drosophila
    • Llamazares, S. et al. polo encodes a protein kinase homolog required for mitosis in Drosophila. Genes Dev. 5, 2153-2165 (1991).
    • (1991) Genes Dev. , vol.5 , pp. 2153-2165
    • Llamazares, S.1
  • 80
    • 0023804548 scopus 로고
    • Polo, a mitotic mutant of Drosophila displaying abnormal spindle poles
    • Sunkel, C. E. & Glover, D. M. polo, a mitotic mutant of Drosophila displaying abnormal spindle poles. J. Cell Sci. 89, 25-38 (1988).
    • (1988) J. Cell Sci. , vol.89 , pp. 25-38
    • Sunkel, C.E.1    Glover, D.M.2
  • 81
    • 0030462914 scopus 로고    scopus 로고
    • Antibody microinjection reveals an essential role for human polo-like kinase 1 (Plk1) in the functional maturation of mitotic centrosomes
    • Lane, H. A. & Nigg, E. A. Antibody microinjection reveals an essential role for human polo-like kinase 1 (Plk1) in the functional maturation of mitotic centrosomes. J. Cell Biol. 135, 1701-1713 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 1701-1713
    • Lane, H.A.1    Nigg, E.A.2
  • 82
    • 0034520085 scopus 로고    scopus 로고
    • Dominant-negative polo-like kinase 1 induces mitotic catastrophe independent of cdc25C function
    • Cogswell, J. P., Brown, C. E., Bisi, J. E. & Neill, S. D. Dominant-negative polo-like kinase 1 induces mitotic catastrophe independent of cdc25C function. Cell Growth Differ. 11, 615-623 (2000).
    • (2000) Cell Growth Differ. , vol.11 , pp. 615-623
    • Cogswell, J.P.1    Brown, C.E.2    Bisi, J.E.3    Neill, S.D.4
  • 83
    • 33644767315 scopus 로고    scopus 로고
    • Normal cells, but not cancer cells, survive severe Plk1 depletion
    • Liu, X., Lei, M. & Erikson, R. L. Normal cells, but not cancer cells, survive severe Plk1 depletion. Mol. Cell. Biol. 26, 2073-2108 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2073-2108
    • Liu, X.1    Lei, M.2    Erikson, R.L.3
  • 84
    • 0037046495 scopus 로고    scopus 로고
    • Downregulation of human polo-like kinase activity by antisense oligonucleotides induces growth inhibition in cancer cells
    • Spankuch-Schmitt, B. et al. Downregulation of human polo-like kinase activity by antisense oligonucleotides induces growth inhibition in cancer cells. Oncogene 21, 3162-3171 (2002).
    • (2002) Oncogene , vol.21 , pp. 3162-3171
    • Spankuch-Schmitt, B.1
  • 85
    • 4444354564 scopus 로고    scopus 로고
    • Identification of human polo-like kinase 1 as a potential therapeutic target in pancreatic cancer
    • Gray, P. J. Jr et al. Identification of human polo-like kinase 1 as a potential therapeutic target in pancreatic cancer. Mol. Cancer Ther. 3, 641-646 (2004).
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 641-646
    • Gray Jr., P.J.1
  • 86
    • 0037132736 scopus 로고    scopus 로고
    • Effect of RNA silencing of polo-like kinase-1 (PLK 1) on apoptosis and spindle formation in human cancer cells
    • Spankuch-Schmitt, B., Bereiter-Hahn, J., Kaufmann, M. & Strebhardt, K. Effect of RNA silencing of polo-like kinase-1 (PLK 1) on apoptosis and spindle formation in human cancer cells. J. Natl Cancer Inst. 94, 1863-1877 (2002).
    • (2002) J. Natl Cancer Inst. , vol.94 , pp. 1863-1877
    • Spankuch-Schmitt, B.1    Bereiter-Hahn, J.2    Kaufmann, M.3    Strebhardt, K.4
  • 87
    • 16344367736 scopus 로고    scopus 로고
    • Silencing of polo-like kinase (Plk) 1 via siRNA causes induction of apoptosis and impairment of mitosis machinery in human prostate cancer cells: Implications for the treatment of prostate cancer
    • Reagan-Shaw, S. & Ahmad, N. Silencing of polo-like kinase (Plk) 1 via siRNA causes induction of apoptosis and impairment of mitosis machinery in human prostate cancer cells: implications for the treatment of prostate cancer. FASEB J. 19, 611-613 (2005).
    • (2005) FASEB J. , vol.19 , pp. 611-613
    • Reagan-Shaw, S.1    Ahmad, N.2
  • 88
    • 20144387142 scopus 로고    scopus 로고
    • Intravesical administration of small interfering RNA targeting PLK-1 successfully prevents the growth of bladder cancer
    • Nogawa, M. et al. Intravesical administration of small interfering RNA targeting PLK-1 successfully prevents the growth of bladder cancer. J. Clin. Invest. 115, 978-985 (2005).
    • (2005) J. Clin. Invest. , vol.115 , pp. 978-985
    • Nogawa, M.1
  • 89
    • 2942544699 scopus 로고    scopus 로고
    • Cancer inhibition in nude mice after systemic application of U6 promoter-driven short hairpin RNAs against PLK1
    • Spankuch, B. et al. Cancer inhibition in nude mice after systemic application of U6 promoter-driven short hairpin RNAs against PLK1. J. Natl Cancer Inst. 96, 862-872 (2004).
    • (2004) J. Natl Cancer Inst. , vol.96 , pp. 862-872
    • Spankuch, B.1
  • 90
    • 0037685280 scopus 로고    scopus 로고
    • Expression profiling reveals off-target gene regulation by RNAi
    • Jackson, A. L. et al. Expression profiling reveals off-target gene regulation by RNAi. Nature Biotechnol. 21, 635-637 (2003).
    • (2003) Nature Biotechnol. , vol.21 , pp. 635-637
    • Jackson, A.L.1
  • 91
    • 10444280878 scopus 로고    scopus 로고
    • Strategies to overcome resistance to targeted protein kinase inhibitors
    • Daub, H., Specht, K. & Ullrich, A. Strategies to overcome resistance to targeted protein kinase inhibitors. Nature Rev. Drug Discov. 3, 1001-1010 (2004).
    • (2004) Nature Rev. Drug Discov. , vol.3 , pp. 1001-1010
    • Daub, H.1    Specht, K.2    Ullrich, A.3
  • 92
    • 0036490442 scopus 로고    scopus 로고
    • Smart drugs: Tyrosine kinase inhibitors in cancer therapy
    • Shawver, L. K., Slamon, D. & Ullrich, A. Smart drugs: tyrosine kinase inhibitors in cancer therapy. Cancer Cell 1, 117-123 (2002).
    • (2002) Cancer Cell , vol.1 , pp. 117-123
    • Shawver, L.K.1    Slamon, D.2    Ullrich, A.3
  • 93
    • 17144393305 scopus 로고    scopus 로고
    • Progress in the discovery of polo-like kinase inhibitors
    • McInnes, C., Mezna, M. & Fischer, P. M. Progress in the discovery of polo-like kinase inhibitors. Curr. Top. Med. Chem. 5, 181-197 (2005).
    • (2005) Curr. Top. Med. Chem. , vol.5 , pp. 181-197
    • McInnes, C.1    Mezna, M.2    Fischer, P.M.3
  • 94
    • 1042287130 scopus 로고    scopus 로고
    • The development and application of methods for activity-based protein profiling
    • Jessani, N. & Cravatt, B. F. The development and application of methods for activity-based protein profiling. Curr. Opin. Chem. Biol. 8, 54-59 (2004).
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 54-59
    • Jessani, N.1    Cravatt, B.F.2
  • 95
    • 0033634827 scopus 로고    scopus 로고
    • Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine
    • Walker, E. H. et al. Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine. Mol. Cell 6, 909-919 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 909-919
    • Walker, E.H.1
  • 96
    • 4444223702 scopus 로고    scopus 로고
    • Molecular pharmacology and antitumor activity of PX-866, a novel inhibitor of phosphoinositide-3-kinase signaling
    • Ihle, N. T. et al. Molecular pharmacology and antitumor activity of PX-866, a novel inhibitor of phosphoinositide-3-kinase signaling. Mol. Cancer Ther. 3, 763-772 (2004).
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 763-772
    • Ihle, N.T.1
  • 97
    • 10344236486 scopus 로고    scopus 로고
    • Aurora-kinase inhibitors as anticancer agents
    • Keen, N. & Taylor, S. Aurora-kinase inhibitors as anticancer agents. Nature Rev. Cancer 4, 927-936 (2004).
    • (2004) Nature Rev. Cancer , vol.4 , pp. 927-936
    • Keen, N.1    Taylor, S.2
  • 98
    • 0346214475 scopus 로고    scopus 로고
    • Discovery of a novel family of CDK inhibitors with the program LIDAEUS: Structural basis for ligand-induced disordering of the activation loop
    • Wu, S. Y. et al. Discovery of a novel family of CDK inhibitors with the program LIDAEUS: structural basis for ligand-induced disordering of the activation loop. Structure. (Camb.) 11, 399-410 (2003).
    • (2003) Structure. (Camb.) , vol.11 , pp. 399-410
    • Wu, S.Y.1
  • 99
    • 0013057087 scopus 로고    scopus 로고
    • Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores
    • Ditchfield, C. et al. Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores. J. Cell Biol. 161, 267-280 (2003).
    • (2003) J. Cell Biol. , vol.161 , pp. 267-280
    • Ditchfield, C.1
  • 100
    • 0038746733 scopus 로고    scopus 로고
    • The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint
    • Hauf, S. et al. The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint. J. Cell Biol. 161, 281-294 (2003).
    • (2003) J. Cell Biol. , vol.161 , pp. 281-294
    • Hauf, S.1
  • 101
    • 2342639645 scopus 로고    scopus 로고
    • VX-680, a potent and selective small-molecule inhibitor of the Aurora kinases, suppresses tumor growth in vivo
    • Harrington, E. A. et al. VX-680, a potent and selective small-molecule inhibitor of the Aurora kinases, suppresses tumor growth in vivo. Nature Med. 10, 262-267 (2004).
    • (2004) Nature Med. , vol.10 , pp. 262-267
    • Harrington, E.A.1
  • 102
    • 4644266184 scopus 로고    scopus 로고
    • Roles of polo-like kinase 1 in the assembly of functional mitotic spindles
    • Sumara, I. et al. Roles of polo-like kinase 1 in the assembly of functional mitotic spindles. Curr. Biol. 14, 1712-1722 (2004).
    • (2004) Curr. Biol. , vol.14 , pp. 1712-1722
    • Sumara, I.1
  • 103
    • 0037672151 scopus 로고    scopus 로고
    • Polo-like kinase 1 regulates Nlp, a centrosome protein involved in microtubule nucleation
    • Casenghi, M. et al. Polo-like kinase 1 regulates Nlp, a centrosome protein involved in microtubule nucleation. Dev. Cell 5, 113-125 (2003).
    • (2003) Dev. Cell , vol.5 , pp. 113-125
    • Casenghi, M.1
  • 104
    • 0842324788 scopus 로고    scopus 로고
    • Recycling the cell cycle: Cyclins revisited
    • Murray, A. W. Recycling the cell cycle: cyclins revisited. Cell 116, 221-234 (2004).
    • (2004) Cell , vol.116 , pp. 221-234
    • Murray, A.W.1
  • 105
    • 0035826154 scopus 로고    scopus 로고
    • Polo-like kinase 1 phosphorylates cyclin B1 and targets it to the nucleus during prophase
    • Toyoshima-Morimoto, F., Taniguchi, E., Shinya, N., Iwamatsu, A. & Nishida, E. Polo-like kinase 1 phosphorylates cyclin B1 and targets it to the nucleus during prophase. Nature 410, 215-220 (2001).
    • (2001) Nature , vol.410 , pp. 215-220
    • Toyoshima-Morimoto, F.1    Taniguchi, E.2    Shinya, N.3    Iwamatsu, A.4    Nishida, E.5
  • 106
    • 0037191929 scopus 로고    scopus 로고
    • Cooperative phosphorylation including the activity of polo-like kinase 1 regulates the subcellular localization of cyclin B1
    • Yuan, J. et al. Cooperative phosphorylation including the activity of polo-like kinase 1 regulates the subcellular localization of cyclin B1. Oncogene 21, 8282-8292 (2002).
    • (2002) Oncogene , vol.21 , pp. 8282-8292
    • Yuan, J.1
  • 107
    • 0037322744 scopus 로고    scopus 로고
    • Active cyclin B1-Cdk1 first appears on centrosomes in prophase
    • Jackman, M., Lindon, C., Nigg, E. A. & Pines, J. Active cyclin B1-Cdk1 first appears on centrosomes in prophase. Nature Cell Biol. 5, 143-148 (2003).
    • (2003) Nature Cell Biol. , vol.5 , pp. 143-148
    • Jackman, M.1    Lindon, C.2    Nigg, E.A.3    Pines, J.4
  • 108
    • 0031806809 scopus 로고    scopus 로고
    • Activated polo-like kinase Plx1 is required at multiple points during mitosis in Xenopus laevis
    • Qian, Y. W., Erikson, E., Li, C. & Mailer, J. L. Activated polo-like kinase Plx1 is required at multiple points during mitosis in Xenopus laevis. Mol. Cell. Biol. 18, 4262-4271 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4262-4271
    • Qian, Y.W.1    Erikson, E.2    Li, C.3    Mailer, J.L.4
  • 109
    • 0036256260 scopus 로고    scopus 로고
    • Plk1 promotes nuclear translocation of human Cdc25C during prophase
    • Toyoshima-Morimoto, F., Taniguchi, E. & Nishida, E. Plk1 promotes nuclear translocation of human Cdc25C during prophase. EMBO Rep. 3, 341-348 (2002).
    • (2002) EMBO Rep. , vol.3 , pp. 341-348
    • Toyoshima-Morimoto, F.1    Taniguchi, E.2    Nishida, E.3
  • 110
    • 12444311754 scopus 로고    scopus 로고
    • Anaphase-promoting complex-dependent proteolysis of cell cycle regulators and genomic instability of cancer cells
    • Wasch, R. & Engelbert, D. Anaphase-promoting complex-dependent proteolysis of cell cycle regulators and genomic instability of cancer cells. Oncogene 24, 1-10 (2005).
    • (2005) Oncogene , vol.24 , pp. 1-10
    • Wasch, R.1    Engelbert, D.2
  • 111
    • 13244283007 scopus 로고    scopus 로고
    • The anaphase-promoting complex: A key factor in the regulation of cell cycle
    • Castro, A., Bernis, C., Vigneron, S., Labbe, J. C. & Lorca, T. The anaphase-promoting complex: a key factor in the regulation of cell cycle. Oncogene 24, 314-325 (2005).
    • (2005) Oncogene , vol.24 , pp. 314-325
    • Castro, A.1    Bernis, C.2    Vigneron, S.3    Labbe, J.C.4    Lorca, T.5
  • 112
    • 2542617641 scopus 로고    scopus 로고
    • Role of Polo-like kinase in the degradation of early mitotic inhibitor 1, a regulator of the anaphase promoting complex/cyclosome
    • Moshe, Y., Boulaire, J., Pagano, M. & Hershko, A. Role of Polo-like kinase in the degradation of early mitotic inhibitor 1, a regulator of the anaphase promoting complex/cyclosome. Proc. Natl Acad. Sci. USA 101, 7937-7942 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7937-7942
    • Moshe, Y.1    Boulaire, J.2    Pagano, M.3    Hershko, A.4
  • 113
    • 9444235650 scopus 로고    scopus 로고
    • PlkI regulates activation of the anaphase promoting complex by phosphorylating and triggering SCFβTrCP-dependent destruction of the APC inhibitor Emi1
    • Hansen, D. V., Loktev, A. V., Ban, K. H. & Jackson, P. K. PlkI regulates activation of the anaphase promoting complex by phosphorylating and triggering SCFβTrCP-dependent destruction of the APC inhibitor Emi1. Mol. Biol. Cell 15, 5623-5634 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5623-5634
    • Hansen, D.V.1    Loktev, A.V.2    Ban, K.H.3    Jackson, P.K.4
  • 114
    • 20544449744 scopus 로고    scopus 로고
    • Polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and modulates the association of spindle-checkpoint proteins at kinetochores
    • Ahonen, L. J. et al. Polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and modulates the association of spindle-checkpoint proteins at kinetochores. Curr. Biol. 15, 1078-1089 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 1078-1089
    • Ahonen, L.J.1
  • 115
    • 4344561301 scopus 로고    scopus 로고
    • Molecular interactions of Polo-like-kinase 1 with the mitotic kinesin-like protein CHO1/MKLP-1
    • Liu, X., Zhou, T., Kuriyama, R. & Erikson, R. L. Molecular interactions of Polo-like-kinase 1 with the mitotic kinesin-like protein CHO1/MKLP-1. J. Cell Sci. 117, 3233-3246 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 3233-3246
    • Liu, X.1    Zhou, T.2    Kuriyama, R.3    Erikson, R.L.4
  • 116
    • 0041885206 scopus 로고    scopus 로고
    • Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is required for cytokinesis
    • Neef, R. et al. Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is required for cytokinesis. J. Cell Biol. 162, 863-875 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 863-875
    • Neef, R.1
  • 117
    • 0038686507 scopus 로고    scopus 로고
    • A role for Plk1 phosphorylation of NudC in cytokinesis
    • Zhou, T., Aumais, J. P., Liu, X., Yu-Lee, L. Y. & Erikson, R. L. A role for Plk1 phosphorylation of NudC in cytokinesis. Dev. Cell 5, 127-138 (2003).
    • (2003) Dev. Cell , vol.5 , pp. 127-138
    • Zhou, T.1    Aumais, J.P.2    Liu, X.3    Yu-Lee, L.Y.4    Erikson, R.L.5
  • 118
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt-protein kinase B ternary complex with GSK3-peptide and AMP-PNP
    • Yang, J. et al. Crystal structure of an activated Akt-protein kinase B ternary complex with GSK3-peptide and AMP-PNP. Nature Struct. Biol. 9, 940-944 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 940-944
    • Yang, J.1
  • 119
    • 0033210869 scopus 로고    scopus 로고
    • Prognostic significance of polo-like kinase expression in esophageal carcinoma
    • Tokumitsu, Y. et al. Prognostic significance of polo-like kinase expression in esophageal carcinoma. Int. J. Oncol. 15, 687-692 (1999).
    • (1999) Int. J. Oncol. , vol.15 , pp. 687-692
    • Tokumitsu, Y.1
  • 120
    • 0033678020 scopus 로고    scopus 로고
    • Polo-like kinase: A novel marker of proliferation: correlation with estrogen-receptor expression in human breast cancer
    • Wolf, G. et al. Polo-like kinase: a novel marker of proliferation: correlation with estrogen-receptor expression in human breast cancer. Pathol. Res. Pract. 196, 753-759 (2000).
    • (2000) Pathol. Res. Pract. , vol.196 , pp. 753-759
    • Wolf, G.1
  • 121
    • 21044443428 scopus 로고    scopus 로고
    • Polo-like kinase isoforms in breast cancer: Expression patterns and prognostic implications
    • Weichert, W. et al. Polo-like kinase isoforms in breast cancer: expression patterns and prognostic implications. Virchows Arch. 446, 442-450 (2005).
    • (2005) Virchows Arch. , vol.446 , pp. 442-450
    • Weichert, W.1
  • 122
    • 0035836079 scopus 로고    scopus 로고
    • Expression of polo-like kinase in ovarian cancer is associated with histological grade and clinical stage
    • Takai, N. et al. Expression of polo-like kinase in ovarian cancer is associated with histological grade and clinical stage. Cancer Lett. 164, 41-49 (2001).
    • (2001) Cancer Lett. , vol.164 , pp. 41-49
    • Takai, N.1
  • 123
    • 0035839314 scopus 로고    scopus 로고
    • Polo-like kinase (PLK) expression in endometrial carcinoma
    • Takai, N. et al. Polo-like kinase (PLK) expression in endometrial carcinoma. Cancer Lett. 169, 41-49 (2001).
    • (2001) Cancer Lett. , vol.169 , pp. 41-49
    • Takai, N.1
  • 125
    • 10744230963 scopus 로고    scopus 로고
    • Polo-like kinase 1 overexpression is an early event in the progression of papillary carcinoma
    • Ito, Y. et al. Polo-like kinase 1 overexpression is an early event in the progression of papillary carcinoma. Br. J. Cancer 90, 414-418 (2004).
    • (2004) Br. J. Cancer , vol.90 , pp. 414-418
    • Ito, Y.1
  • 126
    • 19944376878 scopus 로고    scopus 로고
    • Overexpression of Polo-like kinase 1 is a common and early event in pancreatic cancer
    • Weichert, W. et al. Overexpression of Polo-like kinase 1 is a common and early event in pancreatic cancer. Pancreatology. 5, 259-265 (2005).
    • (2005) Pancreatology , vol.5 , pp. 259-265
    • Weichert, W.1
  • 127
    • 3242792692 scopus 로고    scopus 로고
    • Polo-like kinase 1 is overexpressed in prostate cancer and linked to higher tumor grades
    • Weichert, W. et al. Polo-like kinase 1 is overexpressed in prostate cancer and linked to higher tumor grades. Prostate 60, 240-245 (2004).
    • (2004) Prostate , vol.60 , pp. 240-245
    • Weichert, W.1
  • 128
    • 13244278025 scopus 로고    scopus 로고
    • Expression of Polo-like kinase (PLK1) in non-Hodgkin's lymphomas
    • Mito, K. et al. Expression of Polo-like kinase (PLK1) in non-Hodgkin's lymphomas. Leuk. Lymphoma 46, 225-231 (2005).
    • (2005) Leuk. Lymphoma , vol.46 , pp. 225-231
    • Mito, K.1
  • 129
    • 20844458056 scopus 로고    scopus 로고
    • Chemistry and biology of wortmannin
    • Wipf, P. & Halter, R. J. Chemistry and biology of wortmannin. Org. Biomol. Chem. 3, 2053-2061 (2005).
    • (2005) Org. Biomol. Chem. , vol.3 , pp. 2053-2061
    • Wipf, P.1    Halter, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.