메뉴 건너뛰기




Volumn 7, Issue , 2012, Pages

Therapeutic targeting of cancer cell cycle using proteasome inhibitors

Author keywords

Cancer; Cell cycle; Cell division; Proteasome; Proteasome inhibitors

Indexed keywords


EID: 84871510797     PISSN: None     EISSN: 17471028     Source Type: Journal    
DOI: 10.1186/1747-1028-7-26     Document Type: Review
Times cited : (98)

References (100)
  • 1
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • Hanahan D, Weinberg RA. Hallmarks of cancer: the next generation. Cell 144:646-74.
    • Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 77952507673 scopus 로고    scopus 로고
    • Promises and drawbacks of targeting cell cycle kinases in cancer
    • Pentimalli F, Giordano A. Promises and drawbacks of targeting cell cycle kinases in cancer. Discov Med 2009, 8:177-80.
    • (2009) Discov Med , vol.8 , pp. 177-180
    • Pentimalli, F.1    Giordano, A.2
  • 3
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: a suitable antineoplastic target
    • 10.1038/nrc1361, 15122206
    • Adams J. The proteasome: a suitable antineoplastic target. Nat Rev Cancer 2004, 4:349-60. 10.1038/nrc1361, 15122206.
    • (2004) Nat Rev Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 5
    • 0027516156 scopus 로고
    • Proteasomes: multicatalytic proteinase complexes
    • 1132471, 7682410
    • Rivett AJ. Proteasomes: multicatalytic proteinase complexes. Biochem J 1993, 291(Pt 1):1-10. 1132471, 7682410.
    • (1993) Biochem J , vol.291 , Issue.PART 1 , pp. 1-10
    • Rivett, A.J.1
  • 6
    • 0029071646 scopus 로고
    • Functions of the proteasome: the lysis at the end of the tunnel
    • 10.1126/science.7725095, 7725095
    • Goldberg AL. Functions of the proteasome: the lysis at the end of the tunnel. Science 1995, 268:522-3. 10.1126/science.7725095, 7725095.
    • (1995) Science , vol.268 , pp. 522-523
    • Goldberg, A.L.1
  • 7
    • 0030724422 scopus 로고    scopus 로고
    • Roles of ubiquitin-mediated proteolysis in cell cycle control
    • 10.1016/S0955-0674(97)80079-8, 9425343
    • Hershko A. Roles of ubiquitin-mediated proteolysis in cell cycle control. Curr Opin Cell Biol 1997, 9:788-99. 10.1016/S0955-0674(97)80079-8, 9425343.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 788-799
    • Hershko, A.1
  • 9
    • 0035918278 scopus 로고    scopus 로고
    • Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo
    • 10.1074/jbc.M004209200, 11278274
    • Nam S, Smith DM, Dou QP. Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo. J Biol Chem 2001, 276:13322-30. 10.1074/jbc.M004209200, 11278274.
    • (2001) J Biol Chem , vol.276 , pp. 13322-13330
    • Nam, S.1    Smith, D.M.2    Dou, Q.P.3
  • 10
    • 77952420148 scopus 로고    scopus 로고
    • Proteasome inhibition: a new therapeutic strategy to cancer treatment
    • 10.1016/j.canlet.2009.12.002, 20133049
    • Wu WK, Cho CH, Lee CW, Wu K, Fan D, Yu J, Sung JJ. Proteasome inhibition: a new therapeutic strategy to cancer treatment. Cancer Lett 2010, 293:15-22. 10.1016/j.canlet.2009.12.002, 20133049.
    • (2010) Cancer Lett , vol.293 , pp. 15-22
    • Wu, W.K.1    Cho, C.H.2    Lee, C.W.3    Wu, K.4    Fan, D.5    Yu, J.6    Sung, J.J.7
  • 12
    • 83455238007 scopus 로고    scopus 로고
    • Targeting the ubiquitin-proteasome pathway: an emerging concept in cancer therapy
    • 10.2174/156802611798281311, 21824109
    • Frezza M, Schmitt S, Dou QP. Targeting the ubiquitin-proteasome pathway: an emerging concept in cancer therapy. Curr Top Med Chem 2011, 11:2888-905. 10.2174/156802611798281311, 21824109.
    • (2011) Curr Top Med Chem , vol.11 , pp. 2888-2905
    • Frezza, M.1    Schmitt, S.2    Dou, Q.P.3
  • 13
    • 0036092772 scopus 로고    scopus 로고
    • Proteasome inhibitors: complex tools for a complex enzyme
    • 10.1007/978-3-642-59414-4_8, 12083006
    • Bogyo M, Wang EW. Proteasome inhibitors: complex tools for a complex enzyme. Curr Top Microbiol Immunol 2002, 268:185-208. 10.1007/978-3-642-59414-4_8, 12083006.
    • (2002) Curr Top Microbiol Immunol , vol.268 , pp. 185-208
    • Bogyo, M.1    Wang, E.W.2
  • 16
    • 0345447210 scopus 로고    scopus 로고
    • Velcade: U.S. FDA approval for the treatment of multiple myeloma progressing on prior therapy
    • 10.1634/theoncologist.8-6-508, 14657528
    • Kane RC, Bross PF, Farrell AT, Pazdur R. Velcade: U.S. FDA approval for the treatment of multiple myeloma progressing on prior therapy. Oncologist 2003, 8:508-13. 10.1634/theoncologist.8-6-508, 14657528.
    • (2003) Oncologist , vol.8 , pp. 508-513
    • Kane, R.C.1    Bross, P.F.2    Farrell, A.T.3    Pazdur, R.4
  • 17
    • 33744832401 scopus 로고    scopus 로고
    • United States Food and Drug Administration approval summary: bortezomib for the treatment of progressive multiple myeloma after one prior therapy
    • 10.1158/1078-0432.CCR-06-0170, 16707588
    • Kane RC, Farrell AT, Sridhara R, Pazdur R. United States Food and Drug Administration approval summary: bortezomib for the treatment of progressive multiple myeloma after one prior therapy. Clin Cancer Res 2006, 12:2955-60. 10.1158/1078-0432.CCR-06-0170, 16707588.
    • (2006) Clin Cancer Res , vol.12 , pp. 2955-2960
    • Kane, R.C.1    Farrell, A.T.2    Sridhara, R.3    Pazdur, R.4
  • 18
    • 29244454269 scopus 로고    scopus 로고
    • Bortezomib sensitizes pancreatic cancer cells to endoplasmic reticulum stress-mediated apoptosis
    • 10.1158/0008-5472.CAN-05-2370, 16357177
    • Nawrocki ST, Carew JS, Pino MS, Highshaw RA, Dunner K, Huang P, Abbruzzese JL, McConkey DJ. Bortezomib sensitizes pancreatic cancer cells to endoplasmic reticulum stress-mediated apoptosis. Cancer Res 2005, 65:11658-66. 10.1158/0008-5472.CAN-05-2370, 16357177.
    • (2005) Cancer Res , vol.65 , pp. 11658-11666
    • Nawrocki, S.T.1    Carew, J.S.2    Pino, M.S.3    Highshaw, R.A.4    Dunner, K.5    Huang, P.6    Abbruzzese, J.L.7    McConkey, D.J.8
  • 20
    • 79953678603 scopus 로고    scopus 로고
    • Proteasome inhibition and its therapeutic potential in multiple myeloma
    • 2990320, 21116326
    • Chari A, Mazumder A, Jagannath S. Proteasome inhibition and its therapeutic potential in multiple myeloma. Biologics 2010, 4:273-87. 2990320, 21116326.
    • (2010) Biologics , vol.4 , pp. 273-287
    • Chari, A.1    Mazumder, A.2    Jagannath, S.3
  • 23
    • 64249097600 scopus 로고    scopus 로고
    • Shikonin exerts antitumor activity via proteasome inhibition and cell death induction in vitro and in vivo
    • 10.1002/ijc.24195, 2707765, 19165859
    • Yang H, Zhou P, Huang H, Chen D, Ma N, Cui QC, Shen S, Dong W, Zhang X, Lian W, Wang X, Dou QP, Liu J. Shikonin exerts antitumor activity via proteasome inhibition and cell death induction in vitro and in vivo. Int J Cancer 2009, 124:2450-9. 10.1002/ijc.24195, 2707765, 19165859.
    • (2009) Int J Cancer , vol.124 , pp. 2450-2459
    • Yang, H.1    Zhou, P.2    Huang, H.3    Chen, D.4    Ma, N.5    Cui, Q.C.6    Shen, S.7    Dong, W.8    Zhang, X.9    Lian, W.10    Wang, X.11    Dou, Q.P.12    Liu, J.13
  • 24
    • 54749132655 scopus 로고    scopus 로고
    • Curcumin inhibits the proteasome activity in human colon cancer cells in vitro and in vivo
    • 10.1158/0008-5472.CAN-07-6246, 2556983, 18794115
    • Milacic V, Banerjee S, Landis-Piwowar KR, Sarkar FH, Majumdar AP, Dou QP. Curcumin inhibits the proteasome activity in human colon cancer cells in vitro and in vivo. Cancer Res 2008, 68:7283-92. 10.1158/0008-5472.CAN-07-6246, 2556983, 18794115.
    • (2008) Cancer Res , vol.68 , pp. 7283-7292
    • Milacic, V.1    Banerjee, S.2    Landis-Piwowar, K.R.3    Sarkar, F.H.4    Majumdar, A.P.5    Dou, Q.P.6
  • 25
    • 47349100951 scopus 로고    scopus 로고
    • Natural compounds with proteasome inhibitory activity for cancer prevention and treatment
    • 10.2174/138920308784533998, 3303152, 18537678
    • Yang H, Landis-Piwowar KR, Chen D, Milacic V, Dou QP. Natural compounds with proteasome inhibitory activity for cancer prevention and treatment. Curr Protein Pept Sci 2008, 9:227-39. 10.2174/138920308784533998, 3303152, 18537678.
    • (2008) Curr Protein Pept Sci , vol.9 , pp. 227-239
    • Yang, H.1    Landis-Piwowar, K.R.2    Chen, D.3    Milacic, V.4    Dou, Q.P.5
  • 26
    • 78650733125 scopus 로고    scopus 로고
    • Natural proteasome inhibitor celastrol suppresses androgen-independent prostate cancer progression by modulating apoptotic proteins and NF-kappaB
    • 10.1371/journal.pone.0014153, 3000808, 21170316
    • Dai Y, Desano J, Tang W, Meng X, Meng Y, Burstein E, Lawrence TS, Xu L. Natural proteasome inhibitor celastrol suppresses androgen-independent prostate cancer progression by modulating apoptotic proteins and NF-kappaB. PLoS One 2010, 5:e14153. 10.1371/journal.pone.0014153, 3000808, 21170316.
    • (2010) PLoS One , vol.5
    • Dai, Y.1    Desano, J.2    Tang, W.3    Meng, X.4    Meng, Y.5    Burstein, E.6    Lawrence, T.S.7    Xu, L.8
  • 27
    • 79952924719 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolysis in G1/S phase control and its relationship with tumor susceptibility
    • 10.1177/1947601910382902, 2991141,2991141, 21113395
    • Diehl JA, Ponugoti B. Ubiquitin-dependent proteolysis in G1/S phase control and its relationship with tumor susceptibility. Genes Cancer 2010, 1:717-724. 10.1177/1947601910382902, 2991141,2991141, 21113395.
    • (2010) Genes Cancer , vol.1 , pp. 717-724
    • Diehl, J.A.1    Ponugoti, B.2
  • 28
    • 69249155033 scopus 로고    scopus 로고
    • Cyclin D1 degradation is sufficient to induce G1 cell cycle arrest despite constitutive expression of cyclin E2 in ovarian cancer cells
    • 10.1158/0008-5472.CAN-09-0913, 19638577
    • Masamha CP, Benbrook DM. Cyclin D1 degradation is sufficient to induce G1 cell cycle arrest despite constitutive expression of cyclin E2 in ovarian cancer cells. Cancer Res 2009, 69:6565-72. 10.1158/0008-5472.CAN-09-0913, 19638577.
    • (2009) Cancer Res , vol.69 , pp. 6565-6572
    • Masamha, C.P.1    Benbrook, D.M.2
  • 30
    • 66649117243 scopus 로고    scopus 로고
    • F-box protein FBXO31 mediates cyclin D1 degradation to induce G1 arrest after DNA damage
    • 10.1038/nature08011, 2722223, 19412162
    • Santra MK, Wajapeyee N, Green MR. F-box protein FBXO31 mediates cyclin D1 degradation to induce G1 arrest after DNA damage. Nature 2009, 459:722-5. 10.1038/nature08011, 2722223, 19412162.
    • (2009) Nature , vol.459 , pp. 722-725
    • Santra, M.K.1    Wajapeyee, N.2    Green, M.R.3
  • 31
    • 67649424560 scopus 로고    scopus 로고
    • P21 in cancer: intricate networks and multiple activities
    • 10.1038/nrc2657, 2722839, 19440234
    • Abbas T, Dutta A. p21 in cancer: intricate networks and multiple activities. Nat Rev Cancer 2009, 9:400-14. 10.1038/nrc2657, 2722839, 19440234.
    • (2009) Nat Rev Cancer , vol.9 , pp. 400-414
    • Abbas, T.1    Dutta, A.2
  • 32
    • 41149150219 scopus 로고    scopus 로고
    • The Cdk inhibitor p27 in human cancer: prognostic potential and relevance to anticancer therapy
    • 10.1038/nrc2347, 18354415
    • Chu IM, Hengst L, Slingerland JM. The Cdk inhibitor p27 in human cancer: prognostic potential and relevance to anticancer therapy. Nat Rev Cancer 2008, 8:253-67. 10.1038/nrc2347, 18354415.
    • (2008) Nat Rev Cancer , vol.8 , pp. 253-267
    • Chu, I.M.1    Hengst, L.2    Slingerland, J.M.3
  • 34
    • 79251567380 scopus 로고    scopus 로고
    • Isothiocyanates inhibit proteasome activity and proliferation of multiple myeloma cells
    • 10.1093/carcin/bgq242, 3026846, 21109604
    • Mi L, Gan N, Chung FL. Isothiocyanates inhibit proteasome activity and proliferation of multiple myeloma cells. Carcinogenesis 2011, 32:216-23. 10.1093/carcin/bgq242, 3026846, 21109604.
    • (2011) Carcinogenesis , vol.32 , pp. 216-223
    • Mi, L.1    Gan, N.2    Chung, F.L.3
  • 37
    • 0027109075 scopus 로고
    • Cancer. p53, guardian of the genome
    • 10.1038/358015a0, 1614522
    • Lane DP. Cancer. p53, guardian of the genome. Nature 1992, 358:15-6. 10.1038/358015a0, 1614522.
    • (1992) Nature , vol.358 , pp. 15-16
    • Lane, D.P.1
  • 38
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NFkB1 precursor protein and the activation of NFkB
    • 10.1016/S0092-8674(94)90482-0, 8087845
    • Palombella VJ, Rando OJ, Goldberg AL, Maniatis T. The ubiquitin-proteasome pathway is required for processing the NFkB1 precursor protein and the activation of NFkB. Cell 1994, 78:773-85. 10.1016/S0092-8674(94)90482-0, 8087845.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 39
    • 0037008780 scopus 로고    scopus 로고
    • Evidence that inhibition of p44/42 mitogen-activated protein kinase signaling is a factor in proteasome inhibitor-mediated apoptosis
    • 10.1074/jbc.M201519200, 12023956
    • Orlowski RZ, Small GW, Shi YY. Evidence that inhibition of p44/42 mitogen-activated protein kinase signaling is a factor in proteasome inhibitor-mediated apoptosis. J Biol Chem 2002, 277:27864-71. 10.1074/jbc.M201519200, 12023956.
    • (2002) J Biol Chem , vol.277 , pp. 27864-27871
    • Orlowski, R.Z.1    Small, G.W.2    Shi, Y.Y.3
  • 40
    • 0035736099 scopus 로고    scopus 로고
    • The proteasome: a new target for novel drug therapies
    • 10.1309/44HW-5YCJ-FLLP-3R56, 11710679
    • Elliott PJ, Ross JS. The proteasome: a new target for novel drug therapies. Am J Clin Pathol 2001, 116:637-46. 10.1309/44HW-5YCJ-FLLP-3R56, 11710679.
    • (2001) Am J Clin Pathol , vol.116 , pp. 637-646
    • Elliott, P.J.1    Ross, J.S.2
  • 41
    • 0033578816 scopus 로고    scopus 로고
    • Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1
    • 10.1016/S0092-8674(00)81519-6, 10499802
    • Harbour JW, Luo RX, Dei Santi A, Postigo AA, Dean DC. Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1. Cell 1999, 98:859-69. 10.1016/S0092-8674(00)81519-6, 10499802.
    • (1999) Cell , vol.98 , pp. 859-869
    • Harbour, J.W.1    Luo, R.X.2    Dei Santi, A.3    Postigo, A.A.4    Dean, D.C.5
  • 42
    • 0028970609 scopus 로고
    • Transforming p21ras mutants and c-Ets-2 activate the cyclin D1 promoter through distinguishable regions
    • 10.1074/jbc.270.40.23589, 7559524
    • Albanese C, Johnson J, Watanabe G, Eklund N, Vu D, Arnold A, Pestell RG. Transforming p21ras mutants and c-Ets-2 activate the cyclin D1 promoter through distinguishable regions. J Biol Chem 1995, 270:23589-97. 10.1074/jbc.270.40.23589, 7559524.
    • (1995) J Biol Chem , vol.270 , pp. 23589-23597
    • Albanese, C.1    Johnson, J.2    Watanabe, G.3    Eklund, N.4    Vu, D.5    Arnold, A.6    Pestell, R.G.7
  • 43
    • 0029786329 scopus 로고    scopus 로고
    • Cyclin D1 expression is regulated positively by the p42/p44MAPK and negatively by the p38/HOGMAPK pathway
    • 10.1074/jbc.271.34.20608, 8702807
    • Lavoie JN, L'Allemain G, Brunet A, Muller R, Pouyssegur J. Cyclin D1 expression is regulated positively by the p42/p44MAPK and negatively by the p38/HOGMAPK pathway. J Biol Chem 1996, 271:20608-16. 10.1074/jbc.271.34.20608, 8702807.
    • (1996) J Biol Chem , vol.271 , pp. 20608-20616
    • Lavoie, J.N.1    L'Allemain, G.2    Brunet, A.3    Muller, R.4    Pouyssegur, J.5
  • 44
    • 0029017456 scopus 로고
    • Ras transformation results in an elevated level of cyclin D1 and acceleration of G1 progression in NIH 3 T3 cells
    • 230603, 7791772
    • Liu JJ, Chao JR, Jiang MC, Ng SY, Yen JJ, Yang-Yen HF. Ras transformation results in an elevated level of cyclin D1 and acceleration of G1 progression in NIH 3 T3 cells. Mol Cell Biol 1995, 15:3654-63. 230603, 7791772.
    • (1995) Mol Cell Biol , vol.15 , pp. 3654-3663
    • Liu, J.J.1    Chao, J.R.2    Jiang, M.C.3    Ng, S.Y.4    Yen, J.J.5    Yang-Yen, H.F.6
  • 45
    • 84857368471 scopus 로고    scopus 로고
    • Bortezomib represses HIF-1alpha protein expression and nuclear accumulation by inhibiting both PI3K/Akt/TOR and MAPK pathways in prostate cancer cells
    • Befani CD, Vlachostergios PJ, Hatzidaki E, Patrikidou A, Bonanou S, Simos G, Papandreou CN, Liakos P. Bortezomib represses HIF-1alpha protein expression and nuclear accumulation by inhibiting both PI3K/Akt/TOR and MAPK pathways in prostate cancer cells. J Mol Med (Berl). 2012, 90:45-54.
    • (2012) J Mol Med (Berl). , vol.90 , pp. 45-54
    • Befani, C.D.1    Vlachostergios, P.J.2    Hatzidaki, E.3    Patrikidou, A.4    Bonanou, S.5    Simos, G.6    Papandreou, C.N.7    Liakos, P.8
  • 46
    • 77952757476 scopus 로고    scopus 로고
    • Treatment with p38 inhibitor partially prevents Calu-6 lung cancer cell death by a proteasome inhibitor, MG132
    • 10.1016/j.cancergencyto.2010.02.004, 20471510
    • Han YH, Park WH. Treatment with p38 inhibitor partially prevents Calu-6 lung cancer cell death by a proteasome inhibitor, MG132. Cancer Genet Cytogenet 2010, 199:81-8. 10.1016/j.cancergencyto.2010.02.004, 20471510.
    • (2010) Cancer Genet Cytogenet , vol.199 , pp. 81-88
    • Han, Y.H.1    Park, W.H.2
  • 48
    • 13244262655 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 causes cell growth arrest and apoptosis in human glioblastoma multiforme (GBM)
    • 10.1038/sj.onc.1208225, 15531918
    • Yin D, Zhou H, Kumagai T, Liu G, Ong JM, Black KL, Koeffler HP. Proteasome inhibitor PS-341 causes cell growth arrest and apoptosis in human glioblastoma multiforme (GBM). Oncogene 2005, 24:344-54. 10.1038/sj.onc.1208225, 15531918.
    • (2005) Oncogene , vol.24 , pp. 344-354
    • Yin, D.1    Zhou, H.2    Kumagai, T.3    Liu, G.4    Ong, J.M.5    Black, K.L.6    Koeffler, H.P.7
  • 49
    • 82355175279 scopus 로고    scopus 로고
    • Bortezomib induces autophagy in head and neck squamous cell carcinoma cells via JNK activation
    • 10.1016/j.canlet.2011.09.020, 3225600, 21993018
    • Li C, Johnson DE. Bortezomib induces autophagy in head and neck squamous cell carcinoma cells via JNK activation. Cancer Lett 2012, 314:102-7. 10.1016/j.canlet.2011.09.020, 3225600, 21993018.
    • (2012) Cancer Lett , vol.314 , pp. 102-107
    • Li, C.1    Johnson, D.E.2
  • 50
    • 0033559703 scopus 로고    scopus 로고
    • Regulation of Rb and E2F by signal transduction cascades: divergent effects of JNK1 and p38 kinases
    • 10.1093/emboj/18.6.1559, 1171244, 10075927
    • Wang S, Nath N, Minden A, Chellappan S. Regulation of Rb and E2F by signal transduction cascades: divergent effects of JNK1 and p38 kinases. EMBO J 1999, 18:1559-70. 10.1093/emboj/18.6.1559, 1171244, 10075927.
    • (1999) EMBO J , vol.18 , pp. 1559-1570
    • Wang, S.1    Nath, N.2    Minden, A.3    Chellappan, S.4
  • 51
    • 0033521651 scopus 로고    scopus 로고
    • C-Jun regulates cell cycle progression and apoptosis by distinct mechanisms
    • 10.1093/emboj/18.1.188, 1171114, 9878062
    • Wisdom R, Johnson RS, Moore C. c-Jun regulates cell cycle progression and apoptosis by distinct mechanisms. EMBO J 1999, 18:188-97. 10.1093/emboj/18.1.188, 1171114, 9878062.
    • (1999) EMBO J , vol.18 , pp. 188-197
    • Wisdom, R.1    Johnson, R.S.2    Moore, C.3
  • 53
    • 0026649648 scopus 로고
    • The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
    • 10.1016/0092-8674(92)90644-R, 1535557
    • Momand J, Zambetti GP, Olson DC, George D, Levine AJ. The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell 1992, 69:1237-45. 10.1016/0092-8674(92)90644-R, 1535557.
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 54
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • 10.1038/387296a0, 9153395
    • Haupt Y, Maya R, Kazaz A, Oren M. Mdm2 promotes the rapid degradation of p53. Nature 1997, 387:296-9. 10.1038/387296a0, 9153395.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 55
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • 10.1016/S0014-5793(97)01480-4, 9450543
    • Honda R, Tanaka H, Yasuda H. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett 1997, 420:25-7. 10.1016/S0014-5793(97)01480-4, 9450543.
    • (1997) FEBS Lett , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 56
    • 77449101168 scopus 로고    scopus 로고
    • Mdm2-mediated ubiquitylation: p53 and beyond
    • 10.1038/cdd.2009.68, 19498444
    • Marine JC, Lozano G. Mdm2-mediated ubiquitylation: p53 and beyond. Cell Death Differ 2010, 17:93-102. 10.1038/cdd.2009.68, 19498444.
    • (2010) Cell Death Differ , vol.17 , pp. 93-102
    • Marine, J.C.1    Lozano, G.2
  • 57
    • 0030728767 scopus 로고    scopus 로고
    • The human papillomavirus E7 oncoprotein functionally interacts with the S4 subunit of the 26 S proteasome
    • 10.1074/jbc.272.48.30135, 9374493
    • Berezutskaya E, Bagchi S. The human papillomavirus E7 oncoprotein functionally interacts with the S4 subunit of the 26 S proteasome. J Biol Chem 1997, 272:30135-40. 10.1074/jbc.272.48.30135, 9374493.
    • (1997) J Biol Chem , vol.272 , pp. 30135-30140
    • Berezutskaya, E.1    Bagchi, S.2
  • 58
    • 0031442175 scopus 로고    scopus 로고
    • Differential regulation of the pocket domains of the retinoblastoma family proteins by the HPV16 E7 oncoprotein
    • Berezutskaya E, Yu B, Morozov A, Raychaudhuri P, Bagchi S. Differential regulation of the pocket domains of the retinoblastoma family proteins by the HPV16 E7 oncoprotein. Cell Growth Differ 1997, 8:1277-86.
    • (1997) Cell Growth Differ , vol.8 , pp. 1277-1286
    • Berezutskaya, E.1    Yu, B.2    Morozov, A.3    Raychaudhuri, P.4    Bagchi, S.5
  • 59
    • 0029834371 scopus 로고    scopus 로고
    • E7 protein of human papilloma virus-16 induces degradation of retinoblastoma protein through the ubiquitin-proteasome pathway
    • Boyer SN, Wazer DE, Band V. E7 protein of human papilloma virus-16 induces degradation of retinoblastoma protein through the ubiquitin-proteasome pathway. Cancer Res 1996, 56:4620-4.
    • (1996) Cancer Res , vol.56 , pp. 4620-4624
    • Boyer, S.N.1    Wazer, D.E.2    Band, V.3
  • 60
    • 0035797506 scopus 로고    scopus 로고
    • Both Rb and E7 are regulated by the ubiquitin proteasome pathway in HPV-containing cervical tumor cells
    • 10.1038/sj.onc.1204655, 11498796
    • Wang J, Sampath A, Raychaudhuri P, Bagchi S. Both Rb and E7 are regulated by the ubiquitin proteasome pathway in HPV-containing cervical tumor cells. Oncogene 2001, 20:4740-9. 10.1038/sj.onc.1204655, 11498796.
    • (2001) Oncogene , vol.20 , pp. 4740-4749
    • Wang, J.1    Sampath, A.2    Raychaudhuri, P.3    Bagchi, S.4
  • 61
    • 29444438631 scopus 로고    scopus 로고
    • Epstein-Barr virus latent antigen 3C can mediate the degradation of the retinoblastoma protein through an SCF cellular ubiquitin ligase
    • 10.1073/pnas.0503886102, 1317900, 16352731
    • Knight JS, Sharma N, Robertson ES. Epstein-Barr virus latent antigen 3C can mediate the degradation of the retinoblastoma protein through an SCF cellular ubiquitin ligase. Proc Natl Acad Sci U S A 2005, 102:18562-6. 10.1073/pnas.0503886102, 1317900, 16352731.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 18562-18566
    • Knight, J.S.1    Sharma, N.2    Robertson, E.S.3
  • 62
    • 0033978257 scopus 로고    scopus 로고
    • Reduced stability of retinoblastoma protein by gankyrin, an oncogenic ankyrin-repeat protein overexpressed in hepatomas
    • 10.1038/71600, 10613832
    • Higashitsuji H, Itoh K, Nagao T, Dawson S, Nonoguchi K, Kido T, Mayer RJ, Arii S, Fujita J. Reduced stability of retinoblastoma protein by gankyrin, an oncogenic ankyrin-repeat protein overexpressed in hepatomas. Nat Med 2000, 6:96-9. 10.1038/71600, 10613832.
    • (2000) Nat Med , vol.6 , pp. 96-99
    • Higashitsuji, H.1    Itoh, K.2    Nagao, T.3    Dawson, S.4    Nonoguchi, K.5    Kido, T.6    Mayer, R.J.7    Arii, S.8    Fujita, J.9
  • 63
    • 33644770294 scopus 로고    scopus 로고
    • Targeting retinoblastoma protein for degradation by proteasomes
    • 10.4161/cc.5.5.2515, 16552188
    • Ying H, Xiao ZX. Targeting retinoblastoma protein for degradation by proteasomes. Cell Cycle 2006, 5:506-8. 10.4161/cc.5.5.2515, 16552188.
    • (2006) Cell Cycle , vol.5 , pp. 506-508
    • Ying, H.1    Xiao, Z.X.2
  • 64
    • 77953232989 scopus 로고    scopus 로고
    • Bortezomib decreases Rb phosphorylation and induces caspase-dependent apoptosis in Imatinib-sensitive and -resistant Bcr-Abl1-expressing cells
    • 10.1038/onc.2010.81, 20305692
    • Albero MP, Vaquer JM, Andreu EJ, Villanueva JJ, Franch L, Ivorra C, Poch E, Agirre X, Prosper F, Perez-Roger I. Bortezomib decreases Rb phosphorylation and induces caspase-dependent apoptosis in Imatinib-sensitive and -resistant Bcr-Abl1-expressing cells. Oncogene 2010, 29:3276-86. 10.1038/onc.2010.81, 20305692.
    • (2010) Oncogene , vol.29 , pp. 3276-3286
    • Albero, M.P.1    Vaquer, J.M.2    Andreu, E.J.3    Villanueva, J.J.4    Franch, L.5    Ivorra, C.6    Poch, E.7    Agirre, X.8    Prosper, F.9    Perez-Roger, I.10
  • 66
    • 0030839865 scopus 로고    scopus 로고
    • Oxidative decay of DNA
    • 10.1074/jbc.272.32.19633, 9289489
    • Beckman KB, Ames BN. Oxidative decay of DNA. J Biol Chem 1997, 272:19633-6. 10.1074/jbc.272.32.19633, 9289489.
    • (1997) J Biol Chem , vol.272 , pp. 19633-19636
    • Beckman, K.B.1    Ames, B.N.2
  • 67
    • 18144363210 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors induce DNA damage via reactive oxygen species in human cancer cells
    • 10.1158/0008-5472.CAN-04-2744, 15867362
    • Pan J, She M, Xu ZX, Sun L, Yeung SC. Farnesyltransferase inhibitors induce DNA damage via reactive oxygen species in human cancer cells. Cancer Res 2005, 65:3671-81. 10.1158/0008-5472.CAN-04-2744, 15867362.
    • (2005) Cancer Res , vol.65 , pp. 3671-3681
    • Pan, J.1    She, M.2    Xu, Z.X.3    Sun, L.4    Yeung, S.C.5
  • 68
    • 0030049032 scopus 로고    scopus 로고
    • Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer
    • 1216878, 8546679
    • Wiseman H, Halliwell B. Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer. Biochem J 1996, 313(Pt 1):17-29. 1216878, 8546679.
    • (1996) Biochem J , vol.313 , Issue.PART 1 , pp. 17-29
    • Wiseman, H.1    Halliwell, B.2
  • 69
    • 74849131331 scopus 로고    scopus 로고
    • Butein induces G(2)/M phase arrest and apoptosis in human hepatoma cancer cells through ROS generation
    • 10.1016/j.canlet.2009.07.002, 19643530
    • Moon DO, Kim MO, Choi YH, Hyun JW, Chang WY, Kim GY. Butein induces G(2)/M phase arrest and apoptosis in human hepatoma cancer cells through ROS generation. Cancer Lett 2010, 288:204-13. 10.1016/j.canlet.2009.07.002, 19643530.
    • (2010) Cancer Lett , vol.288 , pp. 204-213
    • Moon, D.O.1    Kim, M.O.2    Choi, Y.H.3    Hyun, J.W.4    Chang, W.Y.5    Kim, G.Y.6
  • 70
    • 0242300088 scopus 로고    scopus 로고
    • Endogenous DNA double-strand breaks: production, fidelity of repair, and induction of cancer
    • 10.1073/pnas.2135498100, 240711, 14566050
    • Vilenchik MM, Knudson AG. Endogenous DNA double-strand breaks: production, fidelity of repair, and induction of cancer. Proc Natl Acad Sci U S A 2003, 100:12871-6. 10.1073/pnas.2135498100, 240711, 14566050.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 12871-12876
    • Vilenchik, M.M.1    Knudson, A.G.2
  • 71
    • 79958695612 scopus 로고    scopus 로고
    • Vorinostat induces reactive oxygen species and DNA damage in acute myeloid leukemia cells
    • 10.1371/journal.pone.0020987, 3112218, 21695163
    • Petruccelli LA, Dupere-Richer D, Pettersson F, Retrouvey H, Skoulikas S, Miller WH. Vorinostat induces reactive oxygen species and DNA damage in acute myeloid leukemia cells. PLoS One 2011, 6:e20987. 10.1371/journal.pone.0020987, 3112218, 21695163.
    • (2011) PLoS One , vol.6
    • Petruccelli, L.A.1    Dupere-Richer, D.2    Pettersson, F.3    Retrouvey, H.4    Skoulikas, S.5    Miller, W.H.6
  • 72
    • 79958211240 scopus 로고    scopus 로고
    • Asperlin induces G/M arrest through ROS generation and ATM pathway in human cervical carcinoma cells
    • 10.1016/j.bbrc.2011.05.032, 21600879
    • He L, Nan MH, Oh HC, Kim YH, Jang JH, Erikson RL, Ahn JS, Kim BY. Asperlin induces G/M arrest through ROS generation and ATM pathway in human cervical carcinoma cells. Biochem Biophys Res Commun 2011, 409:489-93. 10.1016/j.bbrc.2011.05.032, 21600879.
    • (2011) Biochem Biophys Res Commun , vol.409 , pp. 489-493
    • He, L.1    Nan, M.H.2    Oh, H.C.3    Kim, Y.H.4    Jang, J.H.5    Erikson, R.L.6    Ahn, J.S.7    Kim, B.Y.8
  • 76
    • 68249153842 scopus 로고    scopus 로고
    • The effect of MG132, a proteasome inhibitor on HeLa cells in relation to cell growth, reactive oxygen species and GSH
    • Han YH, Moon HJ, You BR, Park WH. The effect of MG132, a proteasome inhibitor on HeLa cells in relation to cell growth, reactive oxygen species and GSH. Oncol Rep 2009, 22:215-21.
    • (2009) Oncol Rep , vol.22 , pp. 215-221
    • Han, Y.H.1    Moon, H.J.2    You, B.R.3    Park, W.H.4
  • 77
    • 33645716061 scopus 로고    scopus 로고
    • P14ARF triggers G2 arrest through ERK-mediated Cdc25C phosphorylation, ubiquitination and proteasomal degradation
    • 10.4161/cc.5.7.2625, 16582626
    • Eymin B, Claverie P, Salon C, Brambilla C, Brambilla E, Gazzeri S. p14ARF triggers G2 arrest through ERK-mediated Cdc25C phosphorylation, ubiquitination and proteasomal degradation. Cell Cycle 2006, 5:759-65. 10.4161/cc.5.7.2625, 16582626.
    • (2006) Cell Cycle , vol.5 , pp. 759-765
    • Eymin, B.1    Claverie, P.2    Salon, C.3    Brambilla, C.4    Brambilla, E.5    Gazzeri, S.6
  • 78
    • 77449097602 scopus 로고    scopus 로고
    • Dissecting the role of ubiquitylation in the DNA damage response checkpoint in G2
    • Bassermann F, Pagano M. Dissecting the role of ubiquitylation in the DNA damage response checkpoint in G2. Cell Death Differ 2011, 17:78-85.
    • (2011) Cell Death Differ , vol.17 , pp. 78-85
    • Bassermann, F.1    Pagano, M.2
  • 79
    • 33749243499 scopus 로고    scopus 로고
    • Proteasome inhibition induces both pro- and anti-cell death pathways in prostate cancer cells
    • 10.1016/j.canlet.2005.11.033, 16413676
    • Yang W, Monroe J, Zhang Y, George D, Bremer E, Li H. Proteasome inhibition induces both pro- and anti-cell death pathways in prostate cancer cells. Cancer Lett 2006, 243:217-27. 10.1016/j.canlet.2005.11.033, 16413676.
    • (2006) Cancer Lett , vol.243 , pp. 217-227
    • Yang, W.1    Monroe, J.2    Zhang, Y.3    George, D.4    Bremer, E.5    Li, H.6
  • 80
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • 10.2353/ajpath.2007.070188, 1934546, 17620365
    • Ding WX, Ni HM, Gao W, Yoshimori T, Stolz DB, Ron D, Yin XM. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am J Pathol 2007, 171:513-24. 10.2353/ajpath.2007.070188, 1934546, 17620365.
    • (2007) Am J Pathol , vol.171 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6    Yin, X.M.7
  • 81
    • 75149175502 scopus 로고    scopus 로고
    • Proteasome inhibitors activate autophagy as a cytoprotective response in human prostate cancer cells
    • 10.1038/onc.2009.343, 2809784, 19881538
    • Zhu K, Dunner K, McConkey DJ. Proteasome inhibitors activate autophagy as a cytoprotective response in human prostate cancer cells. Oncogene 2010, 29:451-62. 10.1038/onc.2009.343, 2809784, 19881538.
    • (2010) Oncogene , vol.29 , pp. 451-462
    • Zhu, K.1    Dunner, K.2    McConkey, D.J.3
  • 82
    • 84855231351 scopus 로고    scopus 로고
    • An autophagy inhibitor enhances the inhibition of cell proliferation
    • Yao F, Wang G, Wei W, Tu Y, Tong H, Sun S. An autophagy inhibitor enhances the inhibition of cell proliferation. Mol Med Report. 2012, 5:84-8.
    • (2012) Mol Med Report. , vol.5 , pp. 84-88
    • Yao, F.1    Wang, G.2    Wei, W.3    Tu, Y.4    Tong, H.5    Sun, S.6
  • 84
    • 84862944939 scopus 로고    scopus 로고
    • Paraptosis accompanied by autophagy and apoptosis was induced by celastrol, a natural compound with influence on proteasome, ER stress and Hsp90
    • 10.1002/jcp.22956, 21866552
    • Wang WB, Feng LX, Yue QX, Wu WY, Guan SH, Jiang BH, Yang M, Liu X, Guo DA. Paraptosis accompanied by autophagy and apoptosis was induced by celastrol, a natural compound with influence on proteasome, ER stress and Hsp90. J Cell Physiol 2012, 227:2196-2206. 10.1002/jcp.22956, 21866552.
    • (2012) J Cell Physiol , vol.227 , pp. 2196-2206
    • Wang, W.B.1    Feng, L.X.2    Yue, Q.X.3    Wu, W.Y.4    Guan, S.H.5    Jiang, B.H.6    Yang, M.7    Liu, X.8    Guo, D.A.9
  • 85
    • 74849136799 scopus 로고    scopus 로고
    • Role of ATF4 in regulation of autophagy and resistance to drugs and hypoxia
    • 10.4161/cc.8.23.10086, 19887912
    • Rzymski T, Milani M, Singleton DC, Harris AL. Role of ATF4 in regulation of autophagy and resistance to drugs and hypoxia. Cell Cycle 2009, 8:3838-47. 10.4161/cc.8.23.10086, 19887912.
    • (2009) Cell Cycle , vol.8 , pp. 3838-3847
    • Rzymski, T.1    Milani, M.2    Singleton, D.C.3    Harris, A.L.4
  • 88
    • 79952016563 scopus 로고    scopus 로고
    • Combined treatment with bortezomib plus bafilomycin A1 enhances the cytocidal effect and induces endoplasmic reticulum stress in U266 myeloma cells: crosstalk among proteasome, autophagy-lysosome and ER stress
    • Kawaguchi T, Miyazawa K, Moriya S, Ohtomo T, Che XF, Naito M, Itoh M, Tomoda A. Combined treatment with bortezomib plus bafilomycin A1 enhances the cytocidal effect and induces endoplasmic reticulum stress in U266 myeloma cells: crosstalk among proteasome, autophagy-lysosome and ER stress. Int J Oncol 2011, 38:643-54.
    • (2011) Int J Oncol , vol.38 , pp. 643-654
    • Kawaguchi, T.1    Miyazawa, K.2    Moriya, S.3    Ohtomo, T.4    Che, X.F.5    Naito, M.6    Itoh, M.7    Tomoda, A.8
  • 89
    • 60549106248 scopus 로고    scopus 로고
    • Inhibition of eIF2alpha dephosphorylation maximizes bortezomib efficiency and eliminates quiescent multiple myeloma cells surviving proteasome inhibitor therapy
    • 10.1158/0008-5472.CAN-08-3858, 2726651, 19190324
    • Schewe DM, Aguirre-Ghiso JA. Inhibition of eIF2alpha dephosphorylation maximizes bortezomib efficiency and eliminates quiescent multiple myeloma cells surviving proteasome inhibitor therapy. Cancer Res 2009, 69:1545-52. 10.1158/0008-5472.CAN-08-3858, 2726651, 19190324.
    • (2009) Cancer Res , vol.69 , pp. 1545-1552
    • Schewe, D.M.1    Aguirre-Ghiso, J.A.2
  • 90
    • 81055149914 scopus 로고    scopus 로고
    • Mechanism of action of proteasome inhibitors and deacetylase inhibitors and the biological basis of synergy in multiple myeloma
    • 10.1158/1535-7163.MCT-11-0433, 22072815
    • Hideshima T, Richardson PG, Anderson KC. Mechanism of action of proteasome inhibitors and deacetylase inhibitors and the biological basis of synergy in multiple myeloma. Mol Cancer Ther 2011, 10:2034-42. 10.1158/1535-7163.MCT-11-0433, 22072815.
    • (2011) Mol Cancer Ther , vol.10 , pp. 2034-2042
    • Hideshima, T.1    Richardson, P.G.2    Anderson, K.C.3
  • 91
    • 49349098483 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: mechanisms of cell death and promise in combination cancer therapy
    • 10.1016/j.canlet.2008.03.037, 18462867
    • Carew JS, Giles FJ, Nawrocki ST. Histone deacetylase inhibitors: mechanisms of cell death and promise in combination cancer therapy. Cancer Lett 2008, 269:7-17. 10.1016/j.canlet.2008.03.037, 18462867.
    • (2008) Cancer Lett , vol.269 , pp. 7-17
    • Carew, J.S.1    Giles, F.J.2    Nawrocki, S.T.3
  • 92
    • 66249124267 scopus 로고    scopus 로고
    • PCI-24781 induces caspase and reactive oxygen species-dependent apoptosis through NF-kappaB mechanisms and is synergistic with bortezomib in lymphoma cells
    • 10.1158/1078-0432.CCR-08-2365, 2704489, 19417023
    • Bhalla S, Balasubramanian S, David K, Sirisawad M, Buggy J, Mauro L, Prachand S, Miller R, Gordon LI, Evens AM. PCI-24781 induces caspase and reactive oxygen species-dependent apoptosis through NF-kappaB mechanisms and is synergistic with bortezomib in lymphoma cells. Clin Cancer Res 2009, 15:3354-65. 10.1158/1078-0432.CCR-08-2365, 2704489, 19417023.
    • (2009) Clin Cancer Res , vol.15 , pp. 3354-3365
    • Bhalla, S.1    Balasubramanian, S.2    David, K.3    Sirisawad, M.4    Buggy, J.5    Mauro, L.6    Prachand, S.7    Miller, R.8    Gordon, L.I.9    Evens, A.M.10
  • 93
    • 80051700467 scopus 로고    scopus 로고
    • Bortezomib targets the caspase-like proteasome activity in cervical cancer cells, triggering apoptosis that can be enhanced by nelfinavir
    • 10.2174/156800911796798913, 21762082
    • Bruning A, Vogel M, Mylonas I, Friese K, Burges A. Bortezomib targets the caspase-like proteasome activity in cervical cancer cells, triggering apoptosis that can be enhanced by nelfinavir. Curr Cancer Drug Targets 2011, 11:799-809. 10.2174/156800911796798913, 21762082.
    • (2011) Curr Cancer Drug Targets , vol.11 , pp. 799-809
    • Bruning, A.1    Vogel, M.2    Mylonas, I.3    Friese, K.4    Burges, A.5
  • 94
    • 34548668194 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor MS-275 alone or combined with bortezomib or sorafenib exhibits strong antiproliferative action in human cholangiocarcinoma cells
    • Baradari V, Hopfner M, Huether A, Schuppan D, Scherubl H. Histone deacetylase inhibitor MS-275 alone or combined with bortezomib or sorafenib exhibits strong antiproliferative action in human cholangiocarcinoma cells. World J Gastroenterol 2007, 13:4458-66.
    • (2007) World J Gastroenterol , vol.13 , pp. 4458-4466
    • Baradari, V.1    Hopfner, M.2    Huether, A.3    Schuppan, D.4    Scherubl, H.5
  • 95
    • 74549173443 scopus 로고    scopus 로고
    • Romidepsin and belinostat synergize the antineoplastic effect of bortezomib in mantle cell lymphoma
    • 10.1158/1078-0432.CCR-09-1937, 20068080
    • Paoluzzi L, Scotto L, Marchi E, Zain J, Seshan VE, O'Connor OA. Romidepsin and belinostat synergize the antineoplastic effect of bortezomib in mantle cell lymphoma. Clin Cancer Res 2010, 16:554-65. 10.1158/1078-0432.CCR-09-1937, 20068080.
    • (2010) Clin Cancer Res , vol.16 , pp. 554-565
    • Paoluzzi, L.1    Scotto, L.2    Marchi, E.3    Zain, J.4    Seshan, V.E.5    O'Connor, O.A.6
  • 96
    • 84856504569 scopus 로고    scopus 로고
    • Antitumor activities of valproic acid on Epstein-Barr virus-associated T and natural killer lymphoma cells
    • 10.1111/j.1349-7006.2011.02127.x, 22017376
    • Iwata S, Saito T, Ito Y, Kamakura M, Gotoh K, Kawada J, Nishiyama Y, Kimura H. Antitumor activities of valproic acid on Epstein-Barr virus-associated T and natural killer lymphoma cells. Cancer Sci 2012, 103:375-81. 10.1111/j.1349-7006.2011.02127.x, 22017376.
    • (2012) Cancer Sci , vol.103 , pp. 375-381
    • Iwata, S.1    Saito, T.2    Ito, Y.3    Kamakura, M.4    Gotoh, K.5    Kawada, J.6    Nishiyama, Y.7    Kimura, H.8
  • 97
    • 78049305999 scopus 로고    scopus 로고
    • MDM2 antagonist Nutlin-3 enhances bortezomib-mediated mitochondrial apoptosis in TP53-mutated mantle cell lymphoma
    • 10.1016/j.canlet.2010.08.015, 20850924
    • Jin L, Tabe Y, Kojima K, Zhou Y, Pittaluga S, Konopleva M, Miida T, Raffeld M. MDM2 antagonist Nutlin-3 enhances bortezomib-mediated mitochondrial apoptosis in TP53-mutated mantle cell lymphoma. Cancer Lett 2010, 299:161-70. 10.1016/j.canlet.2010.08.015, 20850924.
    • (2010) Cancer Lett , vol.299 , pp. 161-170
    • Jin, L.1    Tabe, Y.2    Kojima, K.3    Zhou, Y.4    Pittaluga, S.5    Konopleva, M.6    Miida, T.7    Raffeld, M.8
  • 99
    • 48649105786 scopus 로고    scopus 로고
    • A novel therapeutic combination using PD 0332991 and bortezomib: study in the 5T33MM myeloma model
    • 10.1158/0008-5472.CAN-07-6404, 18632601
    • Menu E, Garcia J, Huang X, Di Liberto M, Toogood PL, Chen I, Vanderkerken K, Chen-Kiang S. A novel therapeutic combination using PD 0332991 and bortezomib: study in the 5T33MM myeloma model. Cancer Res 2008, 68:5519-23. 10.1158/0008-5472.CAN-07-6404, 18632601.
    • (2008) Cancer Res , vol.68 , pp. 5519-5523
    • Menu, E.1    Garcia, J.2    Huang, X.3    Di Liberto, M.4    Toogood, P.L.5    Chen, I.6    Vanderkerken, K.7    Chen-Kiang, S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.