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Volumn 8, Issue 3, 2015, Pages 185-195

Targeting polo-like kinases: A promising therapeutic approac for cancer treatment

Author keywords

[No Author keywords available]

Indexed keywords

CFI 400945; GEMCITABINE; GSK 461364A; GW 843682; MICRORNA 126; POLO LIKE KINASE; POLO LIKE KINASE INHIBITOR; POLOXIN; PROTEIN P53; PURPUROGALLIN; REACTIVE OXYGEN METABOLITE; RIGOSERTIB; TKM 080301; UNCLASSIFIED DRUG; VOLASERTIB;

EID: 84930745615     PISSN: None     EISSN: 19365233     Source Type: Journal    
DOI: 10.1016/j.tranon.2015.03.010     Document Type: Review
Times cited : (149)

References (83)
  • 1
    • 60749109846 scopus 로고    scopus 로고
    • Cell cycle, CDKs and cancer: A changing paradigm
    • Malumbres M and Barbacid M (2009). Cell cycle, CDKs and cancer: a changing paradigm. Nat Rev Cancer 9, 153–166.
    • (2009) Nat Rev Cancer , vol.9 , pp. 153-166
    • Malumbres, M.1    Barbacid, M.2
  • 2
    • 84883183501 scopus 로고    scopus 로고
    • Phospho-Ser/Thr-binding domains: Navigating the cell cycle and DNA damage response
    • [2] Reinhardt HC and Yaffe MB (2013). Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage response. Nat Rev Mol Cell Biol 14, 563–580.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 563-580
    • Reinhardt, H.C.1    Yaffe, M.B.2
  • 3
    • 77955167321 scopus 로고    scopus 로고
    • Multifaceted polo-like kinases: Drug targets and antitargets for cancer therapy
    • [3] Strebhardt K (2010). Multifaceted polo-like kinases: drug targets and antitargets for cancer therapy. Nat Rev Drug Discov 9, 643–660.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 643-660
    • Strebhardt, K.1
  • 4
    • 0023804548 scopus 로고
    • Polo, a mitotic mutant of Drosophila displaying abnormal spindle poles
    • [4] Sunkel CE and Glover DM (1988). Polo, a mitotic mutant of Drosophila displaying abnormal spindle poles. J Cell Sci 89, 25–38.
    • (1988) J Cell Sci , vol.89 , pp. 25-38
    • Sunkel, C.E.1    Glover, D.M.2
  • 5
    • 33645316142 scopus 로고    scopus 로고
    • Targeting polo-like kinase 1 for cancer therapy
    • [5] Strebhardt K and Ullrich A (2006). Targeting polo-like kinase 1 for cancer therapy. Nat Rev Cancer 6, 321–330.
    • (2006) Nat Rev Cancer , vol.6 , pp. 321-330
    • Strebhardt, K.1    Ullrich, A.2
  • 6
    • 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
    • [6] Seong YS, Kamijo K, Lee JS, Fernandez E, Kuriyama R, Miki T, and Lee KS (2002). 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) J Biol Chem , vol.277 , pp. 32282-32293
    • Seong, Y.S.1    Kamijo, K.2    Lee, J.S.3    Fernandez, E.4    Kuriyama, R.5    Miki, T.6    Lee, K.S.7
  • 8
    • 55849147330 scopus 로고    scopus 로고
    • Polo-like kinase 1 is essential for early embryonic development and tumor suppression
    • [8] Lu LY, Wood JL, Minter-Dykhouse K, Ye L, Saunders TL, Yu X, and Chen J (2008). Polo-like kinase 1 is essential for early embryonic development and tumor suppression. Mol Cell Biol 28, 6870–6876.
    • (2008) Mol Cell Biol , vol.28 , pp. 6870-6876
    • Lu, L.Y.1    Wood, J.L.2    Minter-Dykhouse, K.3    Ye, L.4    Saunders, T.L.5    Yu, X.6    Chen, J.7
  • 9
    • 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
    • [9] Lane HA and Nigg EA (1996). 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) J Cell Biol , vol.135 , pp. 1701-1713
    • Lane, H.A.1    Nigg, E.A.2
  • 10
    • 27944453949 scopus 로고    scopus 로고
    • Phosphorylation of Nlp by Plk1 negatively regulates its dynein-dynactin-dependent targeting to the centrosome
    • [10] Casenghi M, Barr FA, and Nigg EA (2005). Phosphorylation of Nlp by Plk1 negatively regulates its dynein-dynactin-dependent targeting to the centrosome. J Cell Sci 118, 5101–5108.
    • (2005) J Cell Sci , vol.118 , pp. 5101-5108
    • Casenghi, M.1    Barr, F.A.2    Nigg, E.A.3
  • 11
    • 32244446180 scopus 로고    scopus 로고
    • A functional interplay between Aurora-A, Plk1 and TPX2 at spindle poles: Plk1 controls centrosomal localization of Aurora-A and TPX2 spindle association
    • [11] De Luca M, Lavia P, and Guarguaglini G (2006). A functional interplay between Aurora-A, Plk1 and TPX2 at spindle poles: Plk1 controls centrosomal localization of Aurora-A and TPX2 spindle association. Cell Cycle 5, 296–303.
    • (2006) Cell Cycle , vol.5 , pp. 296-303
    • De Luca, M.1    Lavia, P.2    Guarguaglini, G.3
  • 12
    • 0034048515 scopus 로고    scopus 로고
    • Imburgia C,FornwaldJ, ScottG,and MarshallLA(2000). The human polo-like kinase, PLK, regulates cdc2/cyclin B through phosphorylation and activation of the cdc25C phosphatase
    • [12] Roshak AK, Capper EA, Imburgia C,FornwaldJ, ScottG,and MarshallLA(2000). The human polo-like kinase, PLK, regulates cdc2/cyclin B through phosphorylation and activation of the cdc25C phosphatase. Cell Signal 12, 405–411.
    • Cell Signal , vol.12 , pp. 405-411
    • Roshak, A.K.1    Capper, E.A.2
  • 13
    • 4444321565 scopus 로고    scopus 로고
    • Polo-like kinase-1 controls recovery from a G2 DNA damage-induced arrest in mammalian cells
    • [13] van Vugt MA, Brás A, and Medema RH (2004). Polo-like kinase-1 controls recovery from a G2 DNA damage-induced arrest in mammalian cells. Mol Cell 15, 799–811.
    • (2004) Mol Cell , vol.15 , pp. 799-811
    • Van Vugt, M.A.1    Brás, A.2    Medema, R.H.3
  • 14
    • 77957041423 scopus 로고    scopus 로고
    • Polo-like kinase 1 phosphorylation of p150Glued facilitates nuclear envelope breakdown during prophase
    • [14] Li H, Liu XS, Yang X, Song B, Wang Y, and Liu X (2010). Polo-like kinase 1 phosphorylation of p150Glued facilitates nuclear envelope breakdown during prophase. Proc Natl Acad Sci U S A 107, 14633–14638.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 14633-14638
    • Li, H.1    Liu, X.S.2    Yang, X.3    Song, B.4    Wang, Y.5    Liu, X.6
  • 16
    • 33751070826 scopus 로고    scopus 로고
    • Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation
    • [16] Kang YH, Park JE, Yu LR, Soung NK, Yun SM, Bang JK, Seong YS, Yu H, Garfield S, and Veenstra TD, et al (2006). Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation. Mol Cell 24, 409–422.
    • (2006) Mol Cell , vol.24 , pp. 409-422
    • Kang, Y.H.1    Park, J.E.2    Yu, L.R.3    Soung, N.K.4    Yun, S.M.5    Bang, J.K.6    Seong, Y.S.7    Yu, H.8    Garfield, S.9    Veenstra, T.D.10
  • 17
    • 77956394930 scopus 로고    scopus 로고
    • Phosphorylation of CLIP-170 by Plk1 and CK2 promotes timely formation of kinetochore-microtubule attachments
    • [17] Li H, Liu XS, Yang X, Wang Y, Wang Y, Turner JR, and Liu X (2010). Phosphorylation of CLIP-170 by Plk1 and CK2 promotes timely formation of kinetochore-microtubule attachments. EMBO J 29, 2953–2965.
    • (2010) EMBO J , vol.29 , pp. 2953-2965
    • Li, H.1    Liu, X.S.2    Yang, X.3    Wang, Y.4    Wang, Y.5    Turner, J.R.6    Liu, X.7
  • 18
    • 84868695288 scopus 로고    scopus 로고
    • Plk1 phosphorylates Sgt1 at the kinetochores to promote timely kinetochore-microtubule attachment
    • [18] Liu XS, Song B, Tang J, Liu W, Kuang S, and Liu X (2012). Plk1 phosphorylates Sgt1 at the kinetochores to promote timely kinetochore-microtubule attachment. Mol Cell Biol 32, 4053–4067.
    • (2012) Mol Cell Biol , vol.32 , pp. 4053-4067
    • Liu, X.S.1    Song, B.2    Tang, J.3    Liu, W.4    Kuang, S.5    Liu, X.6
  • 19
    • 0037013326 scopus 로고    scopus 로고
    • The cyclin-ubiquitin ligase activity of cyclosome/APC is jointly activated by protein kinases Cdk1-cyclin B and Plk
    • [19] Golan A, Yudkovsky Y, and Hershko A (2002). The cyclin-ubiquitin ligase activity of cyclosome/APC is jointly activated by protein kinases Cdk1-cyclin B and Plk. J Biol Chem 277, 15552–15557.
    • (2002) J Biol Chem , vol.277 , pp. 15552-15557
    • Golan, A.1    Yudkovsky, Y.2    Hershko, A.3
  • 20
    • 9444235650 scopus 로고    scopus 로고
    • Plk1 regulates activation of the anaphase promoting complex by phosphorylating and triggering SCFbe-taTrCP-dependent destruction of the APC inhibitor Emi1
    • [20] Hansen DV, Loktev AV, Ban KH, and Jackson PK (2004). Plk1 regulates activation of the anaphase promoting complex by phosphorylating and triggering SCFbe-taTrCP-dependent destruction of the APC inhibitor Emi1. Mol Biol Cell 15, 5623–5634.
    • (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
  • 21
    • 34047119210 scopus 로고    scopus 로고
    • Choice of Plk1 docking partners during mitosis and cytokinesis is controlled by the activation state of Cdk1
    • [21] Neef R, Gruneberg U, Kopajtich R, Li X, Nigg EA, Sillje H, and Barr FA (2007). Choice of Plk1 docking partners during mitosis and cytokinesis is controlled by the activation state of Cdk1. Nat Cell Biol 9, 436–444.
    • (2007) Nat Cell Biol , vol.9 , pp. 436-444
    • Neef, R.1    Gruneberg, U.2    Kopajtich, R.3    Li, X.4    Nigg, E.A.5    Sillje, H.6    Barr, F.A.7
  • 22
    • 66249092744 scopus 로고    scopus 로고
    • Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation
    • [22] Wolfe BA, Takaki T, Petronczki M, and Glotzer M (2009). Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation. PLoS Biol 7, e1000110.
    • (2009) Plos Biol , pp. 7
    • Wolfe, B.A.1    Takaki, T.2    Petronczki, M.3    Glotzer, M.4
  • 23
    • 62849123093 scopus 로고    scopus 로고
    • Polo-like kinases: Conservation and divergence in their functions and regulation
    • [23] Archambault V and Glover DM (2009). Polo-like kinases: conservation and divergence in their functions and regulation. Nat Rev Mol Cell Biol 10, 265–275.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 265-275
    • Archambault, V.1    Glover, D.M.2
  • 25
    • 1642458099 scopus 로고    scopus 로고
    • Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells
    • [25] Lindon C and Pines J (2004). Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells. J Cell Biol 164, 233–241.
    • (2004) J Cell Biol , vol.164 , pp. 233-241
    • Lindon, C.1    Pines, J.2
  • 26
    • 56449109605 scopus 로고    scopus 로고
    • Plk2 regulated centriole duplication is dependent on its localization to the centrioles and a functional polo-box domain
    • [26] Cizmecioglu O, Warnke S, Arnold M, Duensing S, and Hoffmann I (2008). Plk2 regulated centriole duplication is dependent on its localization to the centrioles and a functional polo-box domain. Cell Cycle 7, 3548–3555.
    • (2008) Cell Cycle , vol.7 , pp. 3548-3555
    • Cizmecioglu, O.1    Warnke, S.2    Arnold, M.3    Duensing, S.4    Hoffmann, I.5
  • 27
    • 0042132030 scopus 로고    scopus 로고
    • Silencing of the novel p53 target gene Snk/Plk2 leads to mitotic catastrophe in paclitaxel (taxol)-exposed cells
    • [27] Burns TF, Fei P, Scata KA, Dicker DT, and El-Deiry WS (2003). Silencing of the novel p53 target gene Snk/Plk2 leads to mitotic catastrophe in paclitaxel (taxol)-exposed cells. Mol Cell Biol 23, 5556–5571.
    • (2003) Mol Cell Biol , vol.23 , pp. 5556-5571
    • Burns, T.F.1    Fei, P.2    Scata, K.A.3    Dicker, D.T.4    El-Deiry, W.S.5
  • 28
    • 0141781074 scopus 로고    scopus 로고
    • Role of Plk2 (Snk) in mouse development and cell proliferation
    • [28] Ma S, Charron J, and Erikson RL (2003). Role of Plk2 (Snk) in mouse development and cell proliferation. Mol Cell Biol 23, 6936–6943.
    • (2003) Mol Cell Biol , vol.23 , pp. 6936-6943
    • Ma, S.1    Charron, J.2    Erikson, R.L.3
  • 29
    • 49249127687 scopus 로고    scopus 로고
    • Polo-like kinase 3 functions as a tumor suppressor and is a negative regulator of hypoxia-inducible factor-1 alpha under hypoxic conditions
    • [29] Yang Y, Bai J, Shen R, Brown SA, Komissarova E, Huang Y, Jiang N, Alberts GF, Costa M, and Lu L, et al (2008). Polo-like kinase 3 functions as a tumor suppressor and is a negative regulator of hypoxia-inducible factor-1 alpha under hypoxic conditions. Cancer Res 68, 4077–4085.
    • (2008) Cancer Res , vol.68 , pp. 4077-4085
    • Yang, Y.1    Bai, J.2    Shen, R.3    Brown, S.A.4    Komissarova, E.5    Huang, Y.6    Jiang, N.7    Alberts, G.F.8    Costa, M.9    Lu, L.10
  • 30
    • 33846904706 scopus 로고    scopus 로고
    • Polo-like kinase 3 is required for entry into S phase
    • [30] Zimmerman WC and Erikson RL (2007). Polo-like kinase 3 is required for entry into S phase. Proc Natl Acad Sci U S A 104, 1847–1852.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1847-1852
    • Zimmerman, W.C.1    Erikson, R.L.2
  • 31
    • 33744520878 scopus 로고    scopus 로고
    • Polo box domain of Plk3 functions as a centrosome localization signal, overexpression of which causes mitotic arrest, cytokinesis defects, and apoptosis
    • [31] Jiang N, Wang X, Jhanwar-Uniyal M, Darzynkiewicz Z, and Dai W (2006). Polo box domain of Plk3 functions as a centrosome localization signal, overexpression of which causes mitotic arrest, cytokinesis defects, and apoptosis. J Biol Chem 281, 10577–10582.
    • (2006) J Biol Chem , vol.281 , pp. 10577-10582
    • Jiang, N.1    Wang, X.2    Jhanwar-Uniyal, M.3    Darzynkiewicz, Z.4    Dai, W.5
  • 33
    • 0029743890 scopus 로고    scopus 로고
    • Constitutive expression of murine Sak-a suppresses cell growth and induces multinucleation
    • [33] Fode C, Binkert C, and Dennis JW (1996). Constitutive expression of murine Sak-a suppresses cell growth and induces multinucleation. Mol Cell Biol 16, 4665–4672.
    • (1996) Mol Cell Biol , vol.16 , pp. 4665-4672
    • Fode, C.1    Binkert, C.2    Dennis, J.W.3
  • 35
    • 84890278751 scopus 로고    scopus 로고
    • The role of polo-like kinase 1 in carcinogenesis: Cause or consequence?
    • [35] Cholewa BD, Liu X, and Ahmad N (2013). The role of polo-like kinase 1 in carcinogenesis: cause or consequence? Cancer Res 73, 6848–6855.
    • (2013) Cancer Res , vol.73 , pp. 6848-6855
    • Cholewa, B.D.1    Liu, X.2    Ahmad, N.3
  • 37
    • 84863215537 scopus 로고    scopus 로고
    • Polo like kinase 2 tumour suppressor and cancer biomarker: New perspectives on drug sensitivity/resistance in ovarian cancer
    • [37] Coley HM, Hatzimichael E, Blagden S, McNeish I, Thompson A, Crook T, and Syed N (2012). Polo like kinase 2 tumour suppressor and cancer biomarker: new perspectives on drug sensitivity/resistance in ovarian cancer. Oncotarget 3, 78–83.
    • (2012) Oncotarget , vol.3 , pp. 78-83
    • Coley, H.M.1    Hatzimichael, E.2    Blagden, S.3    McNeish, I.4    Thompson, A.5    Crook, T.6    Syed, N.7
  • 39
    • 0029770725 scopus 로고    scopus 로고
    • Prk, a cytokine-inducible human protein serine/threonine kinase whose expression appears to be down-regulated in lung carcinomas
    • [39] Li B, Ouyang B, Pan H, Reissmann PT, Slamon DJ, Arceci R, Lu L, and Dai W (1996). Prk, a cytokine-inducible human protein serine/threonine kinase whose expression appears to be down-regulated in lung carcinomas. J Biol Chem 271, 19402–19408.
    • (1996) J Biol Chem , vol.271 , pp. 19402-19408
    • Li, B.1    Ouyang, B.2    Pan, H.3    Reissmann, P.T.4    Slamon, D.J.5    Arceci, R.6    Lu, L.7    Dai, W.8
  • 41
    • 0034785447 scopus 로고    scopus 로고
    • Comparative expression of the mitotic regulators SAK and PLK in colorectal cancer
    • [41] Macmillan JC, Hudson JW, Bull S, Dennis JW, and Swallow CJ (2001). Comparative expression of the mitotic regulators SAK and PLK in colorectal cancer. Ann Surg Oncol 8, 729–740.
    • (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
  • 45
    • 67650529837 scopus 로고    scopus 로고
    • Plk1-mediated phosphorylation of Topors regulates p53 stability
    • [45] Yang X, Li H, Zhou Z, Wang WH, Deng A, Andrisani O, and Liu X (2009). Plk1-mediated phosphorylation of Topors regulates p53 stability. J Biol Chem 284, 18588–18592.
    • (2009) J Biol Chem , vol.284 , pp. 18588-18592
    • Yang, X.1    Li, H.2    Zhou, Z.3    Wang, W.H.4    Deng, A.5    Risani, O.6    Liu, X.7
  • 46
    • 77955058029 scopus 로고    scopus 로고
    • Polo-like kinase 1 phosphorylation of G2 and S-phase-expressed 1 protein is essential for p53 inactivation during G2 checkpoint recovery
    • [46] Liu XS, Li H, Song B, and Liu X (2010). Polo-like kinase 1 phosphorylation of G2 and S-phase-expressed 1 protein is essential for p53 inactivation during G2 checkpoint recovery. EMBO Rep 11, 626–632.
    • (2010) EMBO Rep , vol.11 , pp. 626-632
    • Liu, X.S.1    Li, H.2    Song, B.3    Liu, X.4
  • 47
    • 0038624074 scopus 로고    scopus 로고
    • Polo-like kinase (Plk)1 depletion induces apoptosis in cancer cells
    • [47] Liu X and Erikson RL (2003). Polo-like kinase (Plk)1 depletion induces apoptosis in cancer cells. Proc Natl Acad Sci U S A 100, 5789–5794.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 5789-5794
    • Liu, X.1    Erikson, R.L.2
  • 48
    • 33644767315 scopus 로고    scopus 로고
    • Normal cells, but not cancer cells, survive severe Plk1 depletion
    • [48] Liu X, Lei M, and Erikson RL (2006). Normal cells, but not cancer cells, survive severe Plk1 depletion. Mol Cell Biol 26, 2093–2108.
    • (2006) Mol Cell Biol , vol.26 , pp. 2093-2108
    • Liu, X.1    Lei, M.2    Erikson, R.L.3
  • 49
    • 16844369144 scopus 로고    scopus 로고
    • Small interfering RNA-mediated Polo-like kinase 1 depletion preferentially reduces the survival of p53-defective, oncogenic transformed cells and inhibits tumor growth in animals
    • [49] Guan R, Tapang P, Leverson JD, Albert D, Giranda VL, and Luo Y (2005). Small interfering RNA-mediated Polo-like kinase 1 depletion preferentially reduces the survival of p53-defective, oncogenic transformed cells and inhibits tumor growth in animals. Cancer Res 65, 2698–2704.
    • (2005) Cancer Res , vol.65 , pp. 2698-2704
    • Guan, R.1    Tapang, P.2    Leverson, J.D.3    Albert, D.4    Giranda, V.L.5    Luo, Y.6
  • 50
    • 84899562295 scopus 로고    scopus 로고
    • P53-Dependent and cell specific epigenetic regulation of the polo-like kinases under oxidative stress
    • [50] Ward A and Hudson JW (2014). p53-Dependent and cell specific epigenetic regulation of the polo-like kinases under oxidative stress. PLoS One 9, e87918.
    • (2014) Plos One , vol.9
    • Ward, A.1    Hudson, J.W.2
  • 51
    • 0035900745 scopus 로고    scopus 로고
    • Plk3 functionally links DNA damage to cell cycle arrest and apoptosis at least in part via the p53 pathway
    • [51] Xie S, Wu H, Wang Q, Cogswell JP, Husain I, Conn C, Stambrook P, Jhanwar-Uniyal M, and Dai W (2001). Plk3 functionally links DNA damage to cell cycle arrest and apoptosis at least in part via the p53 pathway. J Biol Chem 276, 43305–43312.
    • (2001) J Biol Chem , vol.276 , pp. 43305-43312
    • Xie, S.1    Wu, H.2    Wang, Q.3    Cogswell, J.P.4    Husain, I.5    Conn, C.6    Stambrook, P.7    Jhanwar-Uniyal, M.8    Dai, W.9
  • 52
    • 2942544699 scopus 로고    scopus 로고
    • Cancer inhibition in nude mice after systemic application of U6 promoter-driven short hairpin RNAs against PLK1
    • [52] Spankuch B, Matthess Y, Knecht R, Zimmer B, Kaufmann M, and Strebhardt K (2004). 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) J Natl Cancer Inst , vol.96 , pp. 862-872
    • Spankuch, B.1    Matthess, Y.2    Knecht, R.3    Zimmer, B.4    Kaufmann, M.5    Strebhardt, K.6
  • 53
    • 80053893481 scopus 로고    scopus 로고
    • Polo-like kinase 1 facilitates loss of Pten tumor suppressor-induced prostate cancer formation
    • [53] Liu XS, Song B, Elzey BD, Ratliff TL, Konieczny SF, Cheng L, Ahmad N, and Liu X (2011). Polo-like kinase 1 facilitates loss of Pten tumor suppressor-induced prostate cancer formation. J Biol Chem 286, 35795–35800.
    • (2011) J Biol Chem , vol.286 , pp. 35795-35800
    • Liu, X.S.1    Song, B.2    Elzey, B.D.3    Ratliff, T.L.4    Konieczny, S.F.5    Cheng, L.6    Ahmad, N.7    Liu, X.8
  • 54
    • 79955068894 scopus 로고    scopus 로고
    • Inhibition of polo-like kinase 1 leads to the suppression of osteosarcoma cell growth in vitro and in vivo
    • [54] Liu X, Choy E, Harmon D, Yang S, Yang C, Mankin H, Hornicek FJ, and Duan Z (2011). Inhibition of polo-like kinase 1 leads to the suppression of osteosarcoma cell growth in vitro and in vivo. Anticancer Drugs 22, 444–453.
    • (2011) Anticancer Drugs , vol.22 , pp. 444-453
    • Liu, X.1    Choy, E.2    Harmon, D.3    Yang, S.4    Yang, C.5    Mankin, H.6    Hornicek, F.J.7    Duan, Z.8
  • 61
    • 59049093510 scopus 로고    scopus 로고
    • Deficiency in chromosome congression by the inhibition of Plk1 polo box domain-dependent recognition
    • [61] Watanabe N, Sekine T, Takagi M, Iwasaki J, Imamoto N, Kawasaki H, and Osada H (2009). Deficiency in chromosome congression by the inhibition of Plk1 polo box domain-dependent recognition. J Biol Chem 284, 2344–2353.
    • (2009) J Biol Chem , vol.284 , pp. 2344-2353
    • Watanabe, N.1    Sekine, T.2    Takagi, M.3    Iwasaki, J.4    Imamoto, N.5    Kawasaki, H.6    Osada, H.7
  • 62
    • 43149093993 scopus 로고    scopus 로고
    • Inhibition of polo-like kinase 1 by blocking polo-box domain-dependent protein-protein interactions
    • [62] Reindl W, Yuan J, Kramer A, Strebhardt K, and Berg T (2008). Inhibition of polo-like kinase 1 by blocking polo-box domain-dependent protein-protein interactions. Chem Biol 15, 459–466.
    • (2008) Chem Biol , vol.15 , pp. 459-466
    • Reindl, W.1    Yuan, J.2    Kramer, A.3    Strebhardt, K.4    Berg, T.5
  • 63
  • 64
    • 85019300367 scopus 로고    scopus 로고
    • [64] Reddy EP (2014). Deciphering the novel mechanism of rigosertib. Webcast http://globenewswire.com/news-release/2014/01/17/603196/10064629/en/Onconova-Therapeutics-Inc-to-Host-Webcast-Regarding-Insights-Into-Rigosertib-Mechanism-of-Action-With-Scientific-Founder-Dr-E-Premkumar-Reddy.html; 2014.
    • (2014) Deciphering the Novel Mechanism of Rigosertib
    • Reddy, E.P.1
  • 65
    • 84893249799 scopus 로고    scopus 로고
    • PI3K and cancer: Lessons, challenges and opportunities
    • [65] Fruman DA and Rommel C (2014). PI3K and cancer: lessons, challenges and opportunities. Nat Rev Drug Discov 13, 140–156.
    • (2014) Nat Rev Drug Discov , vol.13 , pp. 140-156
    • Fruman, D.A.1    Rommel, C.2
  • 66
    • 84920698054 scopus 로고    scopus 로고
    • Discovery and development of the Polo-like kinase inhibitor volasertib in cancer therapy
    • [66] Gjertsen BT and Schöffski P (2015). Discovery and development of the Polo-like kinase inhibitor volasertib in cancer therapy. Leukemia 29, 11–19.
    • (2015) Leukemia , vol.29 , pp. 11-19
    • Gjertsen, B.T.1    Schöffski, P.2
  • 67
    • 84900540918 scopus 로고    scopus 로고
    • A phase I study of two dosing schedules of volasertib (BI 6727), an intravenous Polo-like kinase inhibitor, in patients with advanced solid malignancies
    • [67] Lin C-C, Su W, Yen C-J, Hsu C-H, Su W-P, Yeh K-H, Lu Y-S, Cheng AL, Huang DC, and Fritsch H, et al (2014). A phase I study of two dosing schedules of volasertib (BI 6727), an intravenous Polo-like kinase inhibitor, in patients with advanced solid malignancies. Br J Cancer 110, 2434–2440.
    • (2014) Br J Cancer , vol.110 , pp. 2434-2440
    • Lin, C.-C.1    Su, W.2    Yen, C.-J.3    Hsu, C.-H.4    Su, W.-P.5    Yeh, K.-H.6    Lu, Y.-S.7    Cheng, A.L.8    Huang, D.C.9    Fritsch, H.10
  • 68
    • 84655164874 scopus 로고    scopus 로고
    • A phase I, dose-escalation study of the novel Polo-like kinase inhibitor volasertib (BI 6727) in patients with advanced solid tumours
    • [68] Schöffski P, Awada A, Dumez H, Gil T, Bartholomeus S, Wolter P, Taton M, Fritsch H, Glomb P, and Munzert G (2012). A phase I, dose-escalation study of the novel Polo-like kinase inhibitor volasertib (BI 6727) in patients with advanced solid tumours. Eur J Cancer 48, 179–186.
    • (2012) Eur J Cancer , vol.48 , pp. 179-186
    • Schöffski, P.1    Awada, A.2    Dumez, H.3    Gil, T.4    Bartholomeus, S.5    Wolter, P.6    Taton, M.7    Fritsch, H.8    Glomb, P.9    Munzert, G.10
  • 69
    • 84920699404 scopus 로고    scopus 로고
    • Phase I/II study of volasertib, an intravenous Polo-like kinase inhibitor (Plk), in patients with relapsed/refractory acute myeloid leukemia (AML): Updated phase I results for volasertib monotherapy
    • Abstract S649
    • [69] Döhner H, Bug G, Müller-Tidow C, Krämer A, Lübbert M, Krug U, Schlenk RF, Voss F, Taube T, and Liu D, et al (2014). Phase I/II study of volasertib, an intravenous Polo-like kinase inhibitor (Plk), in patients with relapsed/refractory acute myeloid leukemia (AML): updated phase I results for volasertib monotherapy. Haematologica 99 [Abstract S649].
    • (2014) Haematologica , pp. 99
    • Döhner, H.1    Bug, G.2    Müller-Tidow, C.3    Krämer, A.4    Lübbert, M.5    Krug, U.6    Schlenk, R.F.7    Voss, F.8    Taube, T.9    Liu, D.10
  • 70
    • 84884926731 scopus 로고    scopus 로고
    • Cooperative lethality of Polo-like kinases (PLK) and Aurora kinases (AK) in refractory pediatric leukemia
    • Abstract 3573
    • [70] Jayanthan A, Cooper T, Dunn SE, Lewis VA, and Narendran A (2012). Cooperative lethality of Polo-like kinases (PLK) and Aurora kinases (AK) in refractory pediatric leukemia. Blood 120 [Abstract 3573].
    • (2012) Blood , pp. 120
    • Jayanthan, A.1    Cooper, T.2    Dunn, S.E.3    Lewis, V.A.4    Narendran, A.5
  • 71
    • 84907300532 scopus 로고    scopus 로고
    • Randomized, phase 2 trial comparing low-dose cytarabine with or without volasertib in AML patients not suitable for intensive induction therapy
    • [71] Döhner H, Lübbert M, Fiedler W, Fouillard L, Haaland A, Brandwein JM, Lepretre S, Reman O, Turlure P, and Ottmann OG, et al (2014). Randomized, phase 2 trial comparing low-dose cytarabine with or without volasertib in AML patients not suitable for intensive induction therapy. Blood 124, 1426–1433.
    • (2014) Blood , vol.124 , pp. 1426-1433
    • Döhner, H.1    Lübbert, M.2    Fiedler, W.3    Fouillard, L.4    Haaland, A.5    Brandwein, J.M.6    Lepretre, S.7    Reman, O.8    Turlure, P.9    Ottmann, O.G.10
  • 72
    • 84899409111 scopus 로고    scopus 로고
    • An open-label, single-arm, phase 2 trial of the polo-like kinase inhibitor volasertib (BI 6727) in patients with locally advanced or metastatic urothelial cancer
    • [72] Stadler WM, Vaughn DJ, Sonpavde G, Vogelzang NJ, Tagawa ST, Petrylak DP, Rosen P, Lin CC, Mahoney J, and Modi S, et al (2014). An open-label, single-arm, phase 2 trial of the polo-like kinase inhibitor volasertib (BI 6727) in patients with locally advanced or metastatic urothelial cancer. Cancer 120, 976–982.
    • (2014) Cancer , vol.120 , pp. 976-982
    • Stadler, W.M.1    Vaughn, D.J.2    Sonpavde, G.3    Vogelzang, N.J.4    Tagawa, S.T.5    Petrylak, D.P.6    Rosen, P.7    Lin, C.C.8    Mahoney, J.9    Modi, S.10
  • 77
    • 84881425734 scopus 로고    scopus 로고
    • The discovery of PLK4 inhibitors: (E)-3-((1H-Indazol-6-yl)methylene)indolin-2-ones as novel antiproliferative agents
    • [77] Laufer R, Forrest B, Li SW, Liu Y, Sampson P, Edwards L, Lang Y, Awrey DE, Mao G, and Plotnikova O, et al (2013). The discovery of PLK4 inhibitors: (E)-3-((1H-Indazol-6-yl)methylene)indolin-2-ones as novel antiproliferative agents. J Med Chem 56, 6069–6087.
    • (2013) J Med Chem , vol.56 , pp. 6069-6087
    • Laufer, R.1    Forrest, B.2    Li, S.W.3    Liu, Y.4    Sampson, P.5    Edwards, L.6    Lang, Y.7    Awrey, D.E.8    Mao, G.9    Plotnikova, O.10
  • 78
    • 84880709088 scopus 로고    scopus 로고
    • A phase I dose-escalation study of TKM-080301, a RNAi therapeutic directed against polo-like kinase 1 (PLK1), in patients with advanced solid tumors: Expansion cohort evaluation of biopsy samples for evidence of pharmacodynamic effects of PLK1 inhibition
    • Abstract TPS2621
    • [78] Northfelt DW, Hamburg SI, Borad MJ, Seetharam M, Curtis KK, Lee P, Crowell B, Vocila L, Fredlund P, and Gilbert MJ, et al (2013). A phase I dose-escalation study of TKM-080301, a RNAi therapeutic directed against polo-like kinase 1 (PLK1), in patients with advanced solid tumors: Expansion cohort evaluation of biopsy samples for evidence of pharmacodynamic effects of PLK1 inhibition. J Clin Oncol 31 [Abstract TPS2621].
    • (2013) J Clin Oncol , pp. 31
    • Northfelt, D.W.1    Hamburg, S.I.2    Borad, M.J.3    Seetharam, M.4    Curtis, K.K.5    Lee, P.6    Crowell, B.7    Vocila, L.8    Fredlund, P.9    Gilbert, M.J.10
  • 79
    • 85019302111 scopus 로고    scopus 로고
    • KwokR,Ambegia E, and McClintockK,et al(2011). Preclinical characterization of TKM-080301, a lipid nanoparticle formulation of a small interfering RNA directed against polo-like kinase 1
    • [79] Semple SC, Judge AD, Robbins M, Klimuk S, Eisenhardt M, Crosley E, Leung A, KwokR,Ambegia E, and McClintockK,et al(2011). Preclinical characterization of TKM-080301, a lipid nanoparticle formulation of a small interfering RNA directed against polo-like kinase 1. Cancer Res 71, 2829.
    • (2011) Cancer Res , pp. 71
    • Semple, S.C.1    Judge, A.D.2    Robbins, M.3    Klimuk, S.4    Eisenhardt, M.5    Crosley, E.6    Leung, A.7
  • 80
    • 0242556820 scopus 로고    scopus 로고
    • The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex
    • [80] Cheng KY, Lowe ED, Sinclair J, Nigg EA, and Johnson LN (2003). The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex. EMBO J 22, 5757–5768.
    • (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
  • 81
    • 77956624673 scopus 로고    scopus 로고
    • Exploring potential binding modes of small drug-like molecules to the polo-box domain of human polo-like kinase 1
    • [81] Liao C, Park JE, Bang JK, Nicklaus MC, and Lee KS (2010). Exploring potential binding modes of small drug-like molecules to the polo-box domain of human polo-like kinase 1. ACS Med Chem Lett 1, 110–114.
    • (2010) ACS Med Chem Lett , vol.1 , pp. 110-114
    • Liao, C.1    Park, J.E.2    Bang, J.K.3    Nicklaus, M.C.4    Lee, K.S.5
  • 82
  • 83
    • 84885389854 scopus 로고    scopus 로고
    • Current clinical trials with polo-like kinase 1 inhibitors in solid tumors
    • [83] Yim H (2013). Current clinical trials with polo-like kinase 1 inhibitors in solid tumors. Anticancer Drugs 24, 999–1006.
    • (2013) Anticancer Drugs , vol.24 , pp. 999-1006
    • Yim, H.1


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