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Volumn 15, Issue 9, 2016, Pages 2107-2118

Cotargeting HSP90 and its client proteins for treatment of prostate cancer

Author keywords

[No Author keywords available]

Indexed keywords

ANDROGEN RECEPTOR; BETA ACTIN; ENZALUTAMIDE; GELDANAMYCIN; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; LAMIN A; LAMIN C; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; POLO LIKE KINASE 1; PROSTATE SPECIFIC ANTIGEN; TANESPIMYCIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3; ANDROGEN RECEPTOR ANTAGONIST; ANTINEOPLASTIC AGENT; CARRIER PROTEIN; CELL CYCLE PROTEIN; ONCOPROTEIN; POLO-LIKE KINASE 1; PROTEIN BINDING; PROTEIN SERINE THREONINE KINASE;

EID: 84990874015     PISSN: 15357163     EISSN: 15388514     Source Type: Journal    
DOI: 10.1158/1535-7163.MCT-16-0241     Document Type: Article
Times cited : (25)

References (52)
  • 2
    • 84952918413 scopus 로고    scopus 로고
    • Moving beyond the androgen receptor (AR): Targeting AR-interacting proteins to treat prostate cancer
    • Foley C, Mitsiades N. Moving beyond the androgen receptor (AR): Targeting AR-interacting proteins to treat prostate cancer. Horm Cancer 2016;7:84-103.
    • (2016) Horm Cancer , vol.7 , pp. 84-103
    • Foley, C.1    Mitsiades, N.2
  • 3
    • 0028280465 scopus 로고
    • Hormonal therapy for stage D cancer of the prostate
    • Gudziak MR, Smith AY. Hormonal therapy for stage D cancer of the prostate. West J Med 1994;160:351-9.
    • (1994) West J Med , vol.160 , pp. 351-359
    • Gudziak, M.R.1    Smith, A.Y.2
  • 4
    • 35148817305 scopus 로고    scopus 로고
    • Androgen deprivation therapy in the treatment of advanced prostate cancer
    • Perlmutter MA, Lepor H. Androgen deprivation therapy in the treatment of advanced prostate cancer. Rev Urol 2007;9:S3-S8.
    • (2007) Rev Urol , vol.9 , pp. S3-S8
    • Perlmutter, M.A.1    Lepor, H.2
  • 5
    • 84890555121 scopus 로고    scopus 로고
    • Prostate cancer progression after androgen deprivation therapy: Mechanisms of castrate resistance and novel therapeutic approaches
    • Karantanos T, Corn PG, Thompson TC. Prostate cancer progression after androgen deprivation therapy: Mechanisms of castrate resistance and novel therapeutic approaches. Oncogene 2013;32:5501-11.
    • (2013) Oncogene , vol.32 , pp. 5501-5511
    • Karantanos, T.1    Corn, P.G.2    Thompson, T.C.3
  • 6
    • 84858041599 scopus 로고    scopus 로고
    • Androgen receptor signaling in prostate cancer development and progression
    • Lonergan PE, Tindall DJ. Androgen receptor signaling in prostate cancer development and progression. J Carcinog 2011;10:20.
    • (2011) J Carcinog , vol.10 , pp. 20
    • Lonergan, P.E.1    Tindall, D.J.2
  • 7
    • 70749101076 scopus 로고    scopus 로고
    • Steroid hormone receptors in prostate cancer: A hard habit to break?
    • Attard G, Cooper CS, De Bono JS. Steroid hormone receptors in prostate cancer: A hard habit to break? Cancer Cell 2009;16:458-62.
    • (2009) Cancer Cell , vol.16 , pp. 458-462
    • Attard, G.1    Cooper, C.S.2    De Bono, J.S.3
  • 8
    • 78149435915 scopus 로고    scopus 로고
    • Bypass mechanisms of the androgen receptor pathway in therapy-resistant prostate cancer cell models
    • Marques RB, Dits NF, Erkens-Schulze S, Van Weerden WM, Jenster G. Bypass mechanisms of the androgen receptor pathway in therapy-resistant prostate cancer cell models. PLoS ONE 2010;5:e13500.
    • (2010) PLoS ONE , vol.5 , pp. e13500
    • Marques, R.B.1    Dits, N.F.2    Erkens-Schulze, S.3    Van Weerden, W.M.4    Jenster, G.5
  • 10
    • 84941660727 scopus 로고    scopus 로고
    • The wonderous chaperones: A highlight on therapeutics of cancer and potentially malignant disorders
    • Tyagi N, Tyagi R. The wonderous chaperones: A highlight on therapeutics of cancer and potentially malignant disorders. J Oral Maxillofac Pathol 2015;19:212-20.
    • (2015) J Oral Maxillofac Pathol , vol.19 , pp. 212-220
    • Tyagi, N.1    Tyagi, R.2
  • 11
    • 84922032675 scopus 로고    scopus 로고
    • Heat shock protein 90 targeting therapy: State of the art and future perspective
    • Tatokoro M, Koga F, Yoshida S, Kihara K. Heat shock protein 90 targeting therapy: State of the art and future perspective. EXCLI J 2015;14:48-58.
    • (2015) EXCLI J , vol.14 , pp. 48-58
    • Tatokoro, M.1    Koga, F.2    Yoshida, S.3    Kihara, K.4
  • 12
    • 34248187981 scopus 로고    scopus 로고
    • Heat shock protein 90: The cancer chaperone
    • Neckers L. Heat shock protein 90: the cancer chaperone. J Biosci 2007;32:517-30.
    • (2007) J Biosci , vol.32 , pp. 517-530
    • Neckers, L.1
  • 13
    • 79952355328 scopus 로고    scopus 로고
    • High-Content, high-throughput analysis of cell cycle perturbations induced by the HSP90 Inhibitor XL888
    • Lyman SK, Crawley SC, Gong R, Adamkewicz JI, McGrath G, Chew JY, et al. High-Content, high-throughput analysis of cell cycle perturbations induced by the HSP90 Inhibitor XL888. PLoS ONE 2011;6:e17692.
    • (2011) PLoS ONE , vol.6 , pp. e17692
    • Lyman, S.K.1    Crawley, S.C.2    Gong, R.3    Adamkewicz, J.I.4    McGrath, G.5    Chew, J.Y.6
  • 14
    • 0035496220 scopus 로고    scopus 로고
    • The development of androgen-independent prostate cancer
    • Feldman BJ, Feldman D. The development of androgen-independent prostate cancer. Nat Rev Cancer 2001;1:34-45.
    • (2001) Nat Rev Cancer , vol.1 , pp. 34-45
    • Feldman, B.J.1    Feldman, D.2
  • 15
    • 0142125911 scopus 로고    scopus 로고
    • Hsp90 as a therapeutic target in prostate cancer
    • Solit DB, Scher HI, Rosen N. Hsp90 as a therapeutic target in prostate cancer. Sem Oncol 2003;30:709-16.
    • (2003) Sem Oncol , vol.30 , pp. 709-716
    • Solit, D.B.1    Scher, H.I.2    Rosen, N.3
  • 18
    • 0029812759 scopus 로고    scopus 로고
    • Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin
    • Mimnaugh EG, Chavany C, Neckers L. Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J Biol Chem 1996;271:22796-801.
    • (1996) J Biol Chem , vol.271 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3
  • 19
    • 84877925574 scopus 로고    scopus 로고
    • Open-label, dose-escalation, safety, pharmacokinetic, and pharmacodynamic study of intravenously administered CNF1010 (17-(allylamino) - 17-demethoxygeldanamycin [17-AAG]) in patients with solid tumors
    • Saif MW, Erlichman C, Dragovich T, Mendelson D, Toft D, Burrows F, et al. Open-label, dose-escalation, safety, pharmacokinetic, and pharmacodynamic study of intravenously administered CNF1010 (17-(allylamino) - 17-demethoxygeldanamycin [17-AAG]) in patients with solid tumors. Cancer Chemother Pharmacol 2013;71:1345-55.
    • (2013) Cancer Chemother Pharmacol , vol.71 , pp. 1345-1355
    • Saif, M.W.1    Erlichman, C.2    Dragovich, T.3    Mendelson, D.4    Toft, D.5    Burrows, F.6
  • 20
    • 84857050136 scopus 로고    scopus 로고
    • HSP90 as a platform for the assembly of more effective cancer chemotherapy
    • Whitesell L, Lin NU. HSP90 as a platform for the assembly of more effective cancer chemotherapy. Biochim Biophys Acta 2012;1823:756-66.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 756-766
    • Whitesell, L.1    Lin, N.U.2
  • 21
    • 84856217356 scopus 로고    scopus 로고
    • A phase II study of 17-allylamino-17-demethoxygeldanamycin in metastatic or locally advanced, unresectable breast cancer
    • Gartner EM, Silverman P, Simon M, Flaherty L, Abrams J, Ivy P, et al. A phase II study of 17-allylamino-17-demethoxygeldanamycin in metastatic or locally advanced, unresectable breast cancer. Breast Cancer Res Treat 2012;131:933-7.
    • (2012) Breast Cancer Res Treat , vol.131 , pp. 933-937
    • Gartner, E.M.1    Silverman, P.2    Simon, M.3    Flaherty, L.4    Abrams, J.5    Ivy, P.6
  • 22
    • 84856554767 scopus 로고    scopus 로고
    • A Phase II trial of 17-allylamino, 17-demethoxygeldanamycin (17-AAG, tanespimycin) in patients with metastatic melanoma
    • Pacey S, Gore M, Chao D, Banerji U, Larkin J, Sarker S, et al. A Phase II trial of 17-allylamino, 17-demethoxygeldanamycin (17-AAG, tanespimycin) in patients with metastatic melanoma. Invest New Drugs 2012;30:341-9.
    • (2012) Invest New Drugs , vol.30 , pp. 341-349
    • Pacey, S.1    Gore, M.2    Chao, D.3    Banerji, U.4    Larkin, J.5    Sarker, S.6
  • 23
    • 84904543801 scopus 로고    scopus 로고
    • The HSP90 inhibitor ganetespib has chemosensitizer and radiosensitizer activity in colorectal cancer
    • He S, Smith DL, Sequeira M, Sang J, Bates RC, Proia DA. The HSP90 inhibitor ganetespib has chemosensitizer and radiosensitizer activity in colorectal cancer. Invest New Drugs 2014;32:577-86.
    • (2014) Invest New Drugs , vol.32 , pp. 577-586
    • He, S.1    Smith, D.L.2    Sequeira, M.3    Sang, J.4    Bates, R.C.5    Proia, D.A.6
  • 24
    • 43049151493 scopus 로고    scopus 로고
    • Polo on the rise-frommitotic entry to cytokinesis with Plk1
    • Petronczki M, Lénárt P, Peters J-M. Polo on the rise-frommitotic entry to cytokinesis with Plk1. Dev Cell 2008;14:646-59.
    • (2008) Dev Cell , vol.14 , pp. 646-659
    • Petronczki, M.1    Lénárt, P.2    Peters, J.-M.3
  • 25
    • 77955167321 scopus 로고    scopus 로고
    • Multifaceted polo-like kinases: Drug targets and antitargets for cancer therapy
    • Strebhardt K. Multifaceted polo-like kinases: Drug targets and antitargets for cancer therapy. Nat Rev Drug Discov 2010;9:643-60.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 643-660
    • Strebhardt, K.1
  • 26
    • 84918554672 scopus 로고    scopus 로고
    • Plk1 inhibition enhances the efficacy of androgen signaling blockade in castration-resistant prostate cancer
    • Zhang Z, Hou X, Shao C, Li J, Cheng JX, Kuang S, et al. Plk1 inhibition enhances the efficacy of androgen signaling blockade in castration-resistant prostate cancer. Cancer Res 2014;74:6635-47.
    • (2014) Cancer Res , vol.74 , pp. 6635-6647
    • Zhang, Z.1    Hou, X.2    Shao, C.3    Li, J.4    Cheng, J.X.5    Kuang, S.6
  • 27
    • 84906251132 scopus 로고    scopus 로고
    • HSP70 colocalizes with PLK1 at the centrosome and disturbs spindle dynamics in cells arrested in mitosis by arsenic trioxide
    • Chen YJ, Lai KC, Kuo HH, Chow LP, Yih LH, Lee TC. HSP70 colocalizes with PLK1 at the centrosome and disturbs spindle dynamics in cells arrested in mitosis by arsenic trioxide. Arch Toxicol 2014;88:1711-23.
    • (2014) Arch Toxicol , vol.88 , pp. 1711-1723
    • Chen, Y.J.1    Lai, K.C.2    Kuo, H.H.3    Chow, L.P.4    Yih, L.H.5    Lee, T.C.6
  • 28
    • 80055114987 scopus 로고    scopus 로고
    • Proteomic identification of Hsp70 as a new Plk1 substrate in arsenic trioxide-induced mitotically arrested cells
    • Chen YJ, Lin YP, Chow LP, Lee TC. Proteomic identification of Hsp70 as a new Plk1 substrate in arsenic trioxide-induced mitotically arrested cells. Proteomics 2011;11:4331-45.
    • (2011) Proteomics , vol.11 , pp. 4331-4345
    • Chen, Y.J.1    Lin, Y.P.2    Chow, L.P.3    Lee, T.C.4
  • 29
    • 3442890567 scopus 로고    scopus 로고
    • Heat shock protein 90 regulates the metaphase-anaphase transition in a polo-like kinase-dependent manner
    • De Carcer G. Heat shock protein 90 regulates the metaphase-anaphase transition in a polo-like kinase-dependent manner. Cancer Res 2004;64:5106-12.
    • (2004) Cancer Res , vol.64 , pp. 5106-5112
    • De Carcer, G.1
  • 30
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heatshock proteins
    • Connell P, Ballinger CA, Jiang J, Wu Y, Thompson LJ, Hohfeld J, et al. The co-chaperone CHIP regulates protein triage decisions mediated by heatshock proteins. Nat Cell Biol 2001;3:93-6.
    • (2001) Nat Cell Biol , vol.3 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3    Wu, Y.4    Thompson, L.J.5    Hohfeld, J.6
  • 31
    • 73249143709 scopus 로고    scopus 로고
    • Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
    • Kundrat L, Regan L. Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP. J Mol Biol 2010;395:587-94.
    • (2010) J Mol Biol , vol.395 , pp. 587-594
    • Kundrat, L.1    Regan, L.2
  • 32
    • 84879412911 scopus 로고    scopus 로고
    • Cterminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances
    • Muller P, Ruckova E, Halada P, Coates PJ, Hrstka R, Lane DP, et al. Cterminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances. Oncogene 2013;32:3101-10.
    • (2013) Oncogene , vol.32 , pp. 3101-3110
    • Muller, P.1    Ruckova, E.2    Halada, P.3    Coates, P.J.4    Hrstka, R.5    Lane, D.P.6
  • 33
    • 3142672066 scopus 로고    scopus 로고
    • An androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP)
    • He B, Bai S, Hnat AT, Kalman RI, Minges JT, Patterson C, et al. An androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP). J Biol Chem 2004;279:30643-53.
    • (2004) J Biol Chem , vol.279 , pp. 30643-30653
    • He, B.1    Bai, S.2    Hnat, A.T.3    Kalman, R.I.4    Minges, J.T.5    Patterson, C.6
  • 34
    • 33745210533 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase CHIP binds the androgen receptor in a phosphorylation-dependent manner
    • Rees I, Lee S, Kim H, Tsai FT. The E3 ubiquitin ligase CHIP binds the androgen receptor in a phosphorylation-dependent manner. Biochim Biophys Acta 2006;1764:1073-9.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1073-1079
    • Rees, I.1    Lee, S.2    Kim, H.3    Tsai, F.T.4
  • 35
    • 84891745501 scopus 로고    scopus 로고
    • Androgen receptor degradation by the E3 ligase CHIP modulates mitotic arrest in prostate cancer cells
    • Sarkar S, Brautigan DL, Parsons SJ, Larner JM. Androgen receptor degradation by the E3 ligase CHIP modulates mitotic arrest in prostate cancer cells. Oncogene 2014;33:26-33.
    • (2014) Oncogene , vol.33 , pp. 26-33
    • Sarkar, S.1    Brautigan, D.L.2    Parsons, S.J.3    Larner, J.M.4
  • 37
    • 84877686260 scopus 로고    scopus 로고
    • A novel antiandrogen, Compound 30, suppresses castration-resistant and MDV3100-resistant prostate cancer growth in vitro and in vivo
    • Kuruma H, Matsumoto H, Shiota M, Bishop J, Lamoureux F, Thomas C, et al. A novel antiandrogen, Compound 30, suppresses castration-resistant and MDV3100-resistant prostate cancer growth in vitro and in vivo. Mol Cancer Ther 2013;12:567-76.
    • (2013) Mol Cancer Ther , vol.12 , pp. 567-576
    • Kuruma, H.1    Matsumoto, H.2    Shiota, M.3    Bishop, J.4    Lamoureux, F.5    Thomas, C.6
  • 40
    • 84872534568 scopus 로고    scopus 로고
    • Androgen receptor splice variants mediate enzalutamide resistance in castration-resistant prostate cancer cell lines
    • Li Y, Chan SC, Brand LJ, Hwang TH, Silverstein KA, Dehm SM. Androgen receptor splice variants mediate enzalutamide resistance in castration-resistant prostate cancer cell lines. Cancer Res 2013;73:483-9.
    • (2013) Cancer Res , vol.73 , pp. 483-489
    • Li, Y.1    Chan, S.C.2    Brand, L.J.3    Hwang, T.H.4    Silverstein, K.A.5    Dehm, S.M.6
  • 41
    • 78649753203 scopus 로고    scopus 로고
    • The chaperone-dependent ubiquitin ligase CHIP Targets HIF-1a for degradation in the presence of methylglyoxal
    • Bento CF, Fernandes R, Ramalho J, Marques C, Shang F, Taylor A, et al. The chaperone-dependent ubiquitin ligase CHIP Targets HIF-1a for degradation in the presence of methylglyoxal. PLoS ONE 2010;5:e15062.
    • (2010) PLoS ONE , vol.5 , pp. e15062
    • Bento, C.F.1    Fernandes, R.2    Ramalho, J.3    Marques, C.4    Shang, F.5    Taylor, A.6
  • 42
    • 22844447871 scopus 로고    scopus 로고
    • The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation
    • Esser C, Scheffner M, Hohfeld J. The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation. J Biol Chem 2005;280:27443-8.
    • (2005) J Biol Chem , vol.280 , pp. 27443-27448
    • Esser, C.1    Scheffner, M.2    Hohfeld, J.3
  • 43
    • 0347986662 scopus 로고    scopus 로고
    • CHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcription
    • Li L, Xin H, Xu X, Huang M, Zhang X, Chen Y, et al. CHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcription. Mol Cell Biol 2004;24:856-64.
    • (2004) Mol Cell Biol , vol.24 , pp. 856-864
    • Li, L.1    Xin, H.2    Xu, X.3    Huang, M.4    Zhang, X.5    Chen, Y.6
  • 44
    • 84855457952 scopus 로고    scopus 로고
    • Hsp90 molecular chaperone inhibitors: Are we there yet?
    • Neckers L, Workman P. Hsp90 molecular chaperone inhibitors: Are we there yet? Clin Cancer Res 2012;18:64-76.
    • (2012) Clin Cancer Res , vol.18 , pp. 64-76
    • Neckers, L.1    Workman, P.2
  • 45
    • 84855879659 scopus 로고    scopus 로고
    • Cdc28 provides a molecular link between Hsp90, morphogenesis, and cell cycle progression in Candida albicans
    • Senn H, Shapiro RS, Cowen LE. Cdc28 provides a molecular link between Hsp90, morphogenesis, and cell cycle progression in Candida albicans. Mol Biol Cell 2012;23:268-83.
    • (2012) Mol Biol Cell , vol.23 , pp. 268-283
    • Senn, H.1    Shapiro, R.S.2    Cowen, L.E.3
  • 46
    • 84898010148 scopus 로고    scopus 로고
    • Hsp70 and Hsp90 oppositely regulate TGF-beta signaling through CHIP/Stub1
    • Shang Y, Xu X, Duan X, Guo J, Wang Y, Ren F, et al. Hsp70 and Hsp90 oppositely regulate TGF-beta signaling through CHIP/Stub1. Biochem Biophys Res Commun 2014;446:387-92.
    • (2014) Biochem Biophys Res Commun , vol.446 , pp. 387-392
    • Shang, Y.1    Xu, X.2    Duan, X.3    Guo, J.4    Wang, Y.5    Ren, F.6
  • 47
    • 0037148527 scopus 로고    scopus 로고
    • The checkpoint protein Chfr is a ligase that ubiquitinates Plk1 and inhibits Cdc2 at the G2 to M transition
    • Kang D, Chen J, Wong J, Fang G. The checkpoint protein Chfr is a ligase that ubiquitinates Plk1 and inhibits Cdc2 at the G2 to M transition. J Cell Biol 2002;156:249-60.
    • (2002) J Cell Biol , vol.156 , pp. 249-260
    • Kang, D.1    Chen, J.2    Wong, J.3    Fang, G.4
  • 48
    • 84880418571 scopus 로고    scopus 로고
    • CUL3 and protein kinases: Insights from PLK1/KLHL22 interaction
    • Metzger T, Kleiss C, Sumara I. CUL3 and protein kinases: Insights from PLK1/KLHL22 interaction. Cell Cycle 2013;12:2291-6.
    • (2013) Cell Cycle , vol.12 , pp. 2291-2296
    • Metzger, T.1    Kleiss, C.2    Sumara, I.3
  • 50
    • 84921785817 scopus 로고    scopus 로고
    • Inhibition of Pololike Kinase 1 (Plk1) enhances the antineoplastic activity of metformin in prostate cancer
    • Shao C, Ahmad N, Hodges K, Kuang S, Ratliff T, Liu X. Inhibition of Pololike Kinase 1 (Plk1) enhances the antineoplastic activity of metformin in prostate cancer. J Biol Chem 2015;290:2024-33.
    • (2015) J Biol Chem , vol.290 , pp. 2024-2033
    • Shao, C.1    Ahmad, N.2    Hodges, K.3    Kuang, S.4    Ratliff, T.5    Liu, X.6
  • 51
    • 84906952905 scopus 로고    scopus 로고
    • Plk1 Phosphorylation of PTEN causes a tumor-promoting metabolic state
    • Li Z, Li J, Bi P, Lu Y, Burcham G, Elzey BD, et al. Plk1 Phosphorylation of PTEN causes a tumor-promoting metabolic state. Mol Cell Biol 2014;34:3642-61.
    • (2014) Mol Cell Biol , vol.34 , pp. 3642-3661
    • Li, Z.1    Li, J.2    Bi, P.3    Lu, Y.4    Burcham, G.5    Elzey, B.D.6
  • 52
    • 84949661232 scopus 로고    scopus 로고
    • Cotargeting polo-like kinase 1 and the Wnt/beta-catenin signaling pathway in castration-resistant prostate cancer
    • Li J, Karki A, Hodges KB, Ahmad N, Zoubeidi A, Strebhardt K, et al. Cotargeting polo-like kinase 1 and the Wnt/beta-catenin signaling pathway in castration-resistant prostate cancer. Mol Cell Biol 2015;35:4185-98.
    • (2015) Mol Cell Biol , vol.35 , pp. 4185-4198
    • Li, J.1    Karki, A.2    Hodges, K.B.3    Ahmad, N.4    Zoubeidi, A.5    Strebhardt, K.6


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