메뉴 건너뛰기




Volumn 17, Issue 6, 2011, Pages 536-559

Small-molecule inhibitors of p53-MDM2 interaction: The 2006-2010 update

Author keywords

AT 219; Benzodiazepinediones; cis imidazolines; JNJ 26854165; MDM2; MDM2 antagonists; Nutlin; Oxindoles; P53; P53 wild type; Protein protein interaction; RG7112; Smallmolecule anticancer agents; Spiro oxindoles; Spiroindolinone

Indexed keywords

AGENTS AFFECTING PROTEIN METABOLISM; ANTINEOPLASTIC AGENT; AT 219; BORTEZOMIB; DACTINOMYCIN; DOXORUBICIN; ETOPOSIDE; GEMCITABINE; IMATINIB; IMIDAZOLINE DERIVATIVE; INDOLE DERIVATIVE; MI 219; MI 43; MI 63; NSC 3303; NU 8231; NU 8348; NU 8349; NU 8354; NUTLIN 3; PACLITAXEL; PROTEIN MDM2; PROTEIN P53; RG 7112; SERDEMETAN; SJ 172550; UNCLASSIFIED DRUG; UNINDEXED DRUG; VINCRISTINE; WK 23; WW 298;

EID: 79953666206     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161211795222649     Document Type: Review
Times cited : (55)

References (195)
  • 1
    • 0018348655 scopus 로고
    • T antigen is bound to a host protein in SV40-transformed cells
    • Lane DP, Crawford LV. T antigen is bound to a host protein in SV40-transformed cells. Nature 1979; 278: 261-3.
    • (1979) Nature , vol.278 , pp. 261-263
    • Lane, D.P.1    Crawford, L.V.2
  • 2
    • 0018760324 scopus 로고
    • Characterization of a 54K dalton cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells
    • Linzer DI, Levine AJ. Characterization of a 54K dalton cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells. Cell 1979; 17: 43-52.
    • (1979) Cell , vol.17 , pp. 43-52
    • Linzer, D.I.1    Levine, A.J.2
  • 3
    • 0024894289 scopus 로고
    • The p53 tumor suppressor gene and gene product
    • Levine AJ. The p53 tumor suppressor gene and gene product. Princess Takamatsu Symp 1989; 20: 221-30.
    • (1989) Princess Takamatsu Symp , vol.20 , pp. 221-230
    • Levine, A.J.1
  • 4
    • 30344478870 scopus 로고    scopus 로고
    • A global map of p53 transcriptionfactor binding sites in the human genome
    • Wei CL, Wu Q, Vega VB, et al. A global map of p53 transcriptionfactor binding sites in the human genome. Cell 2006; 124: 207-19.
    • (2006) Cell , vol.124 , pp. 207-219
    • Wei, C.L.1    Wu, Q.2    Vega, V.B.3
  • 5
    • 0035496607 scopus 로고    scopus 로고
    • Rescuing the function of mutant p53
    • Bullock AN, Fersht AR. Rescuing the function of mutant p53. Nat Rev Cancer 2001; 1: 68-76.
    • (2001) Nat Rev Cancer , vol.1 , pp. 68-76
    • Bullock, A.N.1    Fersht, A.R.2
  • 7
    • 65949083750 scopus 로고    scopus 로고
    • Cytoplasmic functions of the tumour suppressor p53
    • Green DR, Kroemer G. Cytoplasmic functions of the tumour suppressor p53. Nature 2009; 458: 1127-30.
    • (2009) Nature , vol.458 , pp. 1127-1130
    • Green, D.R.1    Kroemer, G.2
  • 8
    • 77952543499 scopus 로고    scopus 로고
    • The p53 orchestra: Mdm2 and Mdmx set the tone
    • Wade M, Wang YV, Wahl GM. The p53 orchestra: Mdm2 and Mdmx set the tone. Trends Cell Biol 2010; 20: 299-309.
    • (2010) Trends Cell Biol , vol.20 , pp. 299-309
    • Wade, M.1    Wang, Y.V.2    Wahl, G.M.3
  • 9
    • 0023339504 scopus 로고
    • Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line
    • Cahilly-Snyder L, Yang-Feng T, Francke U, George DL. Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line. Somat Cell Mol Genet 1987; 13: 235-44.
    • (1987) Somat Cell Mol Genet , vol.13 , pp. 235-244
    • Cahilly-Snyder, L.1    Yang-Feng, T.2    Francke, U.3    George, D.L.4
  • 10
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, Oren M. Mdm2 promotes the rapid degradation of p53. Nature 1997; 387: 296-9.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 11
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R, Tanaka H, Yasuda H. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett 1997; 420: 25-7.
    • (1997) FEBS Lett , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 12
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat MH, Jones SN, Vousden KH. Regulation of p53 stability by Mdm2. Nature 1997; 387: 299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 14
    • 0026649648 scopus 로고
    • The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
    • 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.
    • (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
  • 15
    • 0032980646 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53
    • Tao W, Levine AJ. Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53. Proc Natl Acad Sci USA 1999; 96: 3077-80.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3077-3080
    • Tao, W.1    Levine, A.J.2
  • 16
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna R, Wagner DS, Lozano G
    • Montes de Oca Luna R, Wagner DS, Lozano G. Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 1995; 378: 203-6.
    • (1995) Nature , vol.378 , pp. 203-206
  • 17
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones SN, Roe AE, Donehower LA, Bradley A. Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 1995; 378: 206-8.
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 19
    • 0037147143 scopus 로고    scopus 로고
    • MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination
    • Badciong JC, Haas AL. MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination. J Biol Chem 2002; 277: 49668-75.
    • (2002) J Biol Chem , vol.277 , pp. 49668-49675
    • Badciong, J.C.1    Haas, A.L.2
  • 20
    • 42149105590 scopus 로고    scopus 로고
    • Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans
    • Linke K, Mace PD, Smith CA, Vaux DL, Silke J, Day CL. Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans. Cell Death Differ 2008; 15: 841-8.
    • (2008) Cell Death Differ , vol.15 , pp. 841-848
    • Linke, K.1    Mace, P.D.2    Smith, C.A.3    Vaux, D.L.4    Silke, J.5    Day, C.L.6
  • 21
    • 10144259344 scopus 로고    scopus 로고
    • MDMX: A novel p53binding protein with some functional properties of MDM2
    • Shvarts A, Steegenga WT, Riteco N, et al. MDMX: a novel p53binding protein with some functional properties of MDM2. EMBO J 1996; 15: 5349-57.
    • (1996) EMBO J , vol.15 , pp. 5349-5357
    • Shvarts, A.1    Steegenga, W.T.2    Riteco, N.3
  • 22
    • 51049098347 scopus 로고    scopus 로고
    • The Arf/p53 pathway in cancer and aging
    • Matheu A, Maraver A, Serrano M. The Arf/p53 pathway in cancer and aging. Cancer Res 2008; 68: 6031-4.
    • (2008) Cancer Res , vol.68 , pp. 6031-6034
    • Matheu, A.1    Maraver, A.2    Serrano, M.3
  • 23
    • 7244238177 scopus 로고    scopus 로고
    • Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5
    • Dai MS, Lu H. Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5. J Biol Chem 2004; 279: 44475-82.
    • (2004) J Biol Chem , vol.279 , pp. 44475-44482
    • Dai, M.S.1    Lu, H.2
  • 24
    • 33747654496 scopus 로고    scopus 로고
    • Regulation of the MDM2-p53 pathway by ribosomal protein L11 involves a post-ubiquitination mechanism
    • Dai MS, Shi D, Jin Y, Sun XX, Zhang Y, Grossman SR, Lu H. Regulation of the MDM2-p53 pathway by ribosomal protein L11 involves a post-ubiquitination mechanism. J Biol Chem 2006; 281: 24304-13.
    • (2006) J Biol Chem , vol.281 , pp. 24304-24313
    • Dai, M.S.1    Shi, D.2    Jin, Y.3    Sun, X.X.4    Zhang, Y.5    Grossman, S.R.6    Lu, H.7
  • 25
    • 4344660471 scopus 로고    scopus 로고
    • Inhibition of HDM2 and activation of p53 by ribosomal protein L23
    • Jin A, Itahana K, O'Keefe K, Zhang Y. Inhibition of HDM2 and activation of p53 by ribosomal protein L23. Mol Cell Biol 2004; 24: 7669-80.
    • (2004) Mol Cell Biol , vol.24 , pp. 7669-7680
    • Jin, A.1    Itahana, K.2    O'Keefe, K.3    Zhang, Y.4
  • 26
    • 0346455772 scopus 로고    scopus 로고
    • Posttranslational modification of MDM2
    • Meek DW, Knippschild U. Posttranslational modification of MDM2. Mol Cancer Res 2003; 1: 1017-26.
    • (2003) Mol Cancer Res , vol.1 , pp. 1017-1026
    • Meek, D.W.1    Knippschild, U.2
  • 27
    • 65549120715 scopus 로고    scopus 로고
    • Modes of p53 regulation
    • Kruse JP, Gu W. Modes of p53 regulation. Cell 2009; 137: 609-22.
    • (2009) Cell , vol.137 , pp. 609-622
    • Kruse, J.P.1    Gu, W.2
  • 28
    • 77449101168 scopus 로고    scopus 로고
    • Mdm2-mediated ubiquitylation: P53 and beyond
    • Marine JC, Lozano G. Mdm2-mediated ubiquitylation: p53 and beyond. Cell Death Differ 2010; 17: 93-102.
    • (2010) Cell Death Differ , vol.17 , pp. 93-102
    • Marine, J.C.1    Lozano, G.2
  • 29
    • 0024387728 scopus 로고
    • Mutations in the p53 gene occur in diverse human tumour types
    • Nigro JM, Baker SJ, Preisinger AC, et al. Mutations in the p53 gene occur in diverse human tumour types. Nature 1989; 342: 705-8.
    • (1989) Nature , vol.342 , pp. 705-708
    • Nigro, J.M.1    Baker, S.J.2    Preisinger, A.C.3
  • 31
    • 0027222956 scopus 로고
    • Mapping of the p53 and mdm-2 interaction domains
    • Chen J, Marechal V, Levine AJ. Mapping of the p53 and mdm-2 interaction domains. Mol Cell Biol 1993; 13: 4107-14.
    • (1993) Mol Cell Biol , vol.13 , pp. 4107-4114
    • Chen, J.1    Marechal, V.2    Levine, A.J.3
  • 33
    • 35148826938 scopus 로고    scopus 로고
    • Shaping genetic alterations in human cancer: The p53 mutation paradigm
    • Soussi T, Wiman KG. Shaping genetic alterations in human cancer: the p53 mutation paradigm. Cancer Cell 2007; 12: 303-12.
    • (2007) Cancer Cell , vol.12 , pp. 303-312
    • Soussi, T.1    Wiman, K.G.2
  • 34
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang S, Jensen JP, Ludwig RL, Vousden KH, Weissman AM. Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J Biol Chem 2000; 275: 8945-51.
    • (2000) J Biol Chem , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 35
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • Kussie PH, Gorina S, Marechal V, et al. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 1996; 274: 948-53.
    • (1996) Science , vol.274 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3
  • 36
    • 0030981049 scopus 로고    scopus 로고
    • A genetic approach to mapping the p53 binding site in the MDM2 protein
    • Freedman DA, Epstein CB, Roth JC, Levine AJ. A genetic approach to mapping the p53 binding site in the MDM2 protein. Mol Med 1997; 3: 248-59.
    • (1997) Mol Med , vol.3 , pp. 248-259
    • Freedman, D.A.1    Epstein, C.B.2    Roth, J.C.3    Levine, A.J.4
  • 37
    • 77952550955 scopus 로고    scopus 로고
    • Small-molecule inhibitors of MDM2 as new anticancer therapeutics
    • Dickens MP, Fitzgerald R, Fischer PM. Small-molecule inhibitors of MDM2 as new anticancer therapeutics. Semin Cancer Biol 2010; 20: 10-8.
    • (2010) Semin Cancer Biol , vol.20 , pp. 10-18
    • Dickens, M.P.1    Fitzgerald, R.2    Fischer, P.M.3
  • 39
    • 33846641698 scopus 로고    scopus 로고
    • Solid-phase synthesis of a library of pyrrolo[2,1c][1,4]benzodiazepine-5,11-diones with potential antitubercular activity
    • Kamal A, Reddy KL, Devaiah V, Shankaraiah N, Reddy GSK, Raghavan S. Solid-phase synthesis of a library of pyrrolo[2,1c][1,4]benzodiazepine-5,11-diones with potential antitubercular activity. J Comb Chem 2007; 9: 29-42.
    • (2007) J Comb Chem , vol.9 , pp. 29-42
    • Kamal, A.1    Reddy, K.L.2    Devaiah, V.3    Shankaraiah, N.4    Reddy, G.S.K.5    Raghavan, S.6
  • 40
    • 0942300602 scopus 로고    scopus 로고
    • Liquid-phase combinatorial synthesis of 1,4-benzodiazepine-2,5-diones as the candidates of endothelin receptor antagonism
    • Cheng M-F, Fang J-M. Liquid-phase combinatorial synthesis of 1,4-benzodiazepine-2,5-diones as the candidates of endothelin receptor antagonism. J Comb Chem 2004; 6: 99-104.
    • (2004) J Comb Chem , vol.6 , pp. 99-104
    • Cheng, M.-F.1    Fang, J.-M.2
  • 41
    • 41649108801 scopus 로고    scopus 로고
    • The 1,4-benzodiazepine2,5-dione small molecule template results in melanocortin receptor agonists with nanomolar potencies
    • Joseph CG, Wilson KR, Wood MS, et al. The 1,4-benzodiazepine2,5-dione small molecule template results in melanocortin receptor agonists with nanomolar potencies. J Med Chem 2008; 51: 1423-1431.
    • (2008) J Med Chem , vol.51 , pp. 1423-1431
    • Joseph, C.G.1    Wilson, K.R.2    Wood, M.S.3
  • 44
    • 0024239320 scopus 로고
    • Methods for drug discovery: Development of potent, selective, orally effective cholecystokinin antagonists
    • Evans BE, Rittle KE, Bock MG, et al. Methods for drug discovery: development of potent, selective, orally effective cholecystokinin antagonists. J Med Chem 1988; 31: 2235-2246.
    • (1988) J Med Chem , vol.31 , pp. 2235-2246
    • Evans, B.E.1    Rittle, K.E.2    Bock, M.G.3
  • 46
    • 34547509909 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of1,4-benzodiazepine-2,5-dione-based HDAC inhibitors
    • Loudni L, Roche J, Potiron V, et al. Design, synthesis and biological evaluation of1,4-benzodiazepine-2,5-dione-based HDAC inhibitors. Bioorg Med Chem Lett 2007; 17: 4819-4823.
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 4819-4823
    • Loudni, L.1    Roche, J.2    Potiron, V.3
  • 47
    • 13944274061 scopus 로고    scopus 로고
    • Discovery and cocrystal structure of benzodiazepinedione HDM2 antagonists that activate p53 in cells
    • Grasberger BL, Lu T, Schubert C, et al. Discovery and cocrystal structure of benzodiazepinedione HDM2 antagonists that activate p53 in cells. J Med Chem 2005; 48: 909-12.
    • (2005) J Med Chem , vol.48 , pp. 909-912
    • Grasberger, B.L.1    Lu, T.2    Schubert, C.3
  • 48
    • 20144382874 scopus 로고    scopus 로고
    • Structure-based design, synthesis, and biological evaluation of novel 1,4-diazepines as HDM2 antagonists
    • Raboisson P, Marugan JJ, Schubert C, et al. Structure-based design, synthesis, and biological evaluation of novel 1,4-diazepines as HDM2 antagonists. Bioorg Med Chem Lett 2005; 15: 1857-61.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 1857-1861
    • Raboisson, P.1    Marugan, J.J.2    Schubert, C.3
  • 49
    • 33144462783 scopus 로고    scopus 로고
    • Patented small molecule inhibitors of p53-MDM2 interaction
    • Deng J, Dayam R, Neamati N. Patented small molecule inhibitors of p53-MDM2 interaction. Expert Opin Ther Pat 2006; 16: 165-88.
    • (2006) Expert Opin Ther Pat , vol.16 , pp. 165-188
    • deng, J.1    Dayam, R.2    Neamati, N.3
  • 50
    • 19944431512 scopus 로고    scopus 로고
    • Calvo RR, et al. 1,4-Benzodiazepine-2,5diones as small molecule antagonists of the HDM2-p53 interaction: Discovery and SAR
    • Parks DJ, Lafrance LV, Calvo RR, et al. 1,4-Benzodiazepine-2,5diones as small molecule antagonists of the HDM2-p53 interaction: discovery and SAR. Bioorg Med Chem Lett 2005; 15: 765-70.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 765-770
    • Parks, D.J.1    Lafrance, L.V.2
  • 51
    • 33747115474 scopus 로고    scopus 로고
    • Enantiomerically pure 1,4-benzodiazepine-2,5-diones as Hdm2 antagonists
    • Marugan JJ, Leonard K, Raboisson P, et al. Enantiomerically pure 1,4-benzodiazepine-2,5-diones as Hdm2 antagonists. Bioorg Med Chem Lett 2006; 16: 3115-20.
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 3115-3120
    • Marugan, J.J.1    Leonard, K.2    Raboisson, P.3
  • 52
    • 58149401867 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the p53-HDM2 interaction for the treatment of cancer
    • Patel S, Player MR. Small-molecule inhibitors of the p53-HDM2 interaction for the treatment of cancer. Expert Opin Investig Drugs 2008; 17: 1865-82.
    • (2008) Expert Opin Investig Drugs , vol.17 , pp. 1865-1882
    • Patel, S.1    Player, M.R.2
  • 53
    • 33747126523 scopus 로고    scopus 로고
    • Enhanced pharmacokinetic properties of 1,4-benzodiazepine-2,5-dione antagonists of the HDM2-p53 protein-protein interaction through structure-based drug design
    • Parks DJ, LaFrance LV, Calvo RR, et al. Enhanced pharmacokinetic properties of 1,4-benzodiazepine-2,5-dione antagonists of the HDM2-p53 protein-protein interaction through structure-based drug design. Bioorg Med Chem Lett 2006; 16: 3310-4.
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 3310-3314
    • Parks, D.J.1    Lafrance, L.V.2    Calvo, R.R.3
  • 54
    • 33746627694 scopus 로고    scopus 로고
    • Novel 1,4benzodiazepine-2,5-diones as Hdm2 antagonists with improved cellular activity
    • Leonard K, Marugan JJ, Raboisson P, et al. Novel 1,4benzodiazepine-2,5-diones as Hdm2 antagonists with improved cellular activity. Bioorg Med Chem Lett 2006; 16: 3463-8.
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 3463-3468
    • Leonard, K.1    Marugan, J.J.2    Raboisson, P.3
  • 55
    • 33644873086 scopus 로고    scopus 로고
    • Benzodiazepinedione inhibitors of the Hdm2:P53 complex suppress human tumor cell proliferation in vitro and sensitize tumors to doxorubicin in vivo
    • Koblish HK, Zhao S, Franks CF, et al. Benzodiazepinedione inhibitors of the Hdm2:p53 complex suppress human tumor cell proliferation in vitro and sensitize tumors to doxorubicin in vivo. Mol Cancer Ther 2006; 5: 160-9.
    • (2006) Mol Cancer Ther , vol.5 , pp. 160-169
    • Koblish, H.K.1    Zhao, S.2    Franks, C.F.3
  • 56
    • 33645357208 scopus 로고    scopus 로고
    • Substituted 1,4benzodiazepine-2,5-diones as alpha-helix mimetic antagonists of the HDM2-p53 protein-protein interaction
    • Cummings MD, Schubert C, Parks DJ, et al. Substituted 1,4benzodiazepine-2,5-diones as alpha-helix mimetic antagonists of the HDM2-p53 protein-protein interaction. Chem Biol Drug Des 2006; 67: 201-5.
    • (2006) Chem Biol Drug Des , vol.67 , pp. 201-205
    • Cummings, M.D.1    Schubert, C.2    Parks, D.J.3
  • 57
    • 77954366814 scopus 로고    scopus 로고
    • Bista M, et al. 1,4-Thienodiazepine-2,5-diones via MCR (I): Synthesis, virtual space and p53-Mdm2 activity
    • Huang Y, Wolf S, Bista M, et al. 1,4-Thienodiazepine-2,5-diones via MCR (I): synthesis, virtual space and p53-Mdm2 activity. Chem Biol Drug Des 2010; 76: 116-29.
    • (2010) Chem Biol Drug Des , vol.76 , pp. 116-129
    • Huang, Y.1    Wolf, S.2
  • 58
    • 53049108040 scopus 로고    scopus 로고
    • Targeting the MDM2-p53 interaction for cancer therapy
    • Shangary S, Wang S. Targeting the MDM2-p53 interaction for cancer therapy. Clin Cancer Res 2008; 14: 5318-24.
    • (2008) Clin Cancer Res , vol.14 , pp. 5318-5324
    • Shangary, S.1    Wang, S.2
  • 59
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev LT, Vu BT, Graves B, et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 2004; 303: 844-8.
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3
  • 60
    • 36048965144 scopus 로고    scopus 로고
    • Exploration of liquid and supercritical fluid chromatographic chiral separation and purification of Nutlin-3--a small molecule antagonist of MDM2
    • Wang Z, Jonca M, Lambros T, Ferguson S, Goodnow R. Exploration of liquid and supercritical fluid chromatographic chiral separation and purification of Nutlin-3--a small molecule antagonist of MDM2. J Pharm Biomed Anal 2007; 45: 720-9.
    • (2007) J Pharm Biomed Anal , vol.45 , pp. 720-729
    • Wang, Z.1    Jonca, M.2    Lambros, T.3    Ferguson, S.4    Goodnow, R.5
  • 62
    • 27744487598 scopus 로고    scopus 로고
    • Nongenotoxic activation of the p53 pathway as a therapeutic strategy for multiple myeloma
    • Stuhmer T, Chatterjee M, Hildebrandt M, et al. Nongenotoxic activation of the p53 pathway as a therapeutic strategy for multiple myeloma. Blood 2005; 106: 3609-17.
    • (2005) Blood , vol.106 , pp. 3609-3617
    • Stuhmer, T.1    Chatterjee, M.2    Hildebrandt, M.3
  • 63
    • 42349085572 scopus 로고    scopus 로고
    • MDM2 antagonist nutlin-3 is a potent inducer of apoptosis in pediatric acute lymphoblastic leukemia cells with wild-type p53 and overexpression of MDM2
    • Gu L, Zhu N, Findley HW, Zhou M. MDM2 antagonist nutlin-3 is a potent inducer of apoptosis in pediatric acute lymphoblastic leukemia cells with wild-type p53 and overexpression of MDM2. Leukemia 2008; 22: 730-9.
    • (2008) Leukemia , vol.22 , pp. 730-739
    • Gu, L.1    Zhu, N.2    Findley, H.W.3    Zhou, M.4
  • 64
    • 27644568226 scopus 로고    scopus 로고
    • MDM2 antagonists induce p53-dependent apoptosis in AML: Implications for leukemia therapy
    • Kojima K, Konopleva M, Samudio IJ, et al. MDM2 antagonists induce p53-dependent apoptosis in AML: implications for leukemia therapy. Blood 2005; 106: 3150-9.
    • (2005) Blood , vol.106 , pp. 3150-3159
    • Kojima, K.1    Konopleva, M.2    Samudio, I.J.3
  • 65
    • 33646550549 scopus 로고    scopus 로고
    • MDM2 antagonists activate p53 and synergize with genotoxic drugs in Bcell chronic lymphocytic leukemia cells
    • Coll-Mulet L, Iglesias-Serret D, Santidrian AF, et al. MDM2 antagonists activate p53 and synergize with genotoxic drugs in Bcell chronic lymphocytic leukemia cells. Blood 2006; 107: 4109-14.
    • (2006) Blood , vol.107 , pp. 4109-4114
    • Coll-Mulet, L.1    Iglesias-Serret, D.2    Santidrian, A.F.3
  • 66
    • 33646574651 scopus 로고    scopus 로고
    • Functional integrity of the p53-mediated apoptotic pathway induced by the nongenotoxic agent nutlin-3 in B-cell chronic lymphocytic leukemia (B-CLL)
    • Secchiero P, Barbarotto E, Tiribelli M, et al. Functional integrity of the p53-mediated apoptotic pathway induced by the nongenotoxic agent nutlin-3 in B-cell chronic lymphocytic leukemia (B-CLL). Blood 2006; 107: 4122-9.
    • (2006) Blood , vol.107 , pp. 4122-4129
    • Secchiero, P.1    Barbarotto, E.2    Tiribelli, M.3
  • 67
    • 43549085043 scopus 로고    scopus 로고
    • The pre-clinical development of MDM2 inhibitors in chronic lymphocytic leukemia uncovers a central role for p53 status in sensitivity to MDM2 inhibitor-mediated apoptosis
    • Bixby D, Kujawski L, Wang S, Malek SN. The pre-clinical development of MDM2 inhibitors in chronic lymphocytic leukemia uncovers a central role for p53 status in sensitivity to MDM2 inhibitor-mediated apoptosis. Cell Cycle 2008; 7: 971-9.
    • (2008) Cell Cycle , vol.7 , pp. 971-979
    • Bixby, D.1    Kujawski, L.2    Wang, S.3    Malek, S.N.4
  • 68
    • 38949135181 scopus 로고    scopus 로고
    • Comprehensive biomarker and genomic analysis identifies p53 status as the major determinant of response to MDM2 inhibitors in chronic lymphocytic leukemia
    • Saddler C, Ouillette P, Kujawski L, et al. Comprehensive biomarker and genomic analysis identifies p53 status as the major determinant of response to MDM2 inhibitors in chronic lymphocytic leukemia. Blood 2008; 111: 1584-93.
    • (2008) Blood , vol.111 , pp. 1584-1593
    • Saddler, C.1    Ouillette, P.2    Kujawski, L.3
  • 69
    • 34250669968 scopus 로고    scopus 로고
    • Inhibition of p53murine double minute 2 interaction by nutlin-3A stabilizes p53 and induces cell cycle arrest and apoptosis in Hodgkin lymphoma
    • Drakos E, Thomaides A, Medeiros LJ, et al. Inhibition of p53murine double minute 2 interaction by nutlin-3A stabilizes p53 and induces cell cycle arrest and apoptosis in Hodgkin lymphoma. Clin Cancer Res 2007; 13: 3380-7.
    • (2007) Clin Cancer Res , vol.13 , pp. 3380-3387
    • Drakos, E.1    Thomaides, A.2    Medeiros, L.J.3
  • 70
    • 77954157430 scopus 로고    scopus 로고
    • Low-dose mithramycin exerts its anticancer effect via the p53 signaling pathway and synergizes with nutlin-3 in gynecologic cancers
    • Ohgami T, Kato K, Kobayashi H, et al. Low-dose mithramycin exerts its anticancer effect via the p53 signaling pathway and synergizes with nutlin-3 in gynecologic cancers. Cancer Sci 2010; 101: 1387-95.
    • (2010) Cancer Sci , vol.101 , pp. 1387-1395
    • Ohgami, T.1    Kato, K.2    Kobayashi, H.3
  • 71
    • 78650439014 scopus 로고    scopus 로고
    • Contrasting effects of nutlin-3 on TRAILand docetaxel-induced apoptosis due to upregulation of TRAIL-R2 and Mcl-1 in human melanoma cells
    • Tseng HY, Jiang CC, Croft A, et al. Contrasting effects of nutlin-3 on TRAILand docetaxel-induced apoptosis due to upregulation of TRAIL-R2 and Mcl-1 in human melanoma cells. Mol Cancer Ther 2010; 9: 3363-74.
    • (2010) Mol Cancer Ther , vol.9 , pp. 3363-3374
    • Tseng, H.Y.1    Jiang, C.C.2    Croft, A.3
  • 72
    • 77956062176 scopus 로고    scopus 로고
    • Nutlin-3 cooperates with doxorubicin to induce apoptosis of human hepatocellular carcinoma cells through p53 or p73 signaling pathways
    • Zheng T, Wang J, Song X, et al. Nutlin-3 cooperates with doxorubicin to induce apoptosis of human hepatocellular carcinoma cells through p53 or p73 signaling pathways. J Cancer Res Clin Oncol 2010; 136: 1597-604.
    • (2010) J Cancer Res Clin Oncol , vol.136 , pp. 1597-1604
    • Zheng, T.1    Wang, J.2    Song, X.3
  • 73
    • 79551512486 scopus 로고    scopus 로고
    • Minn I, et al. p53-Reactivating small molecules induce apoptosis and enhance chemotherapeutic cytotoxicity in head and neck squamous cell carcinoma
    • Roh JL, Kang SK, Minn I, et al. p53-Reactivating small molecules induce apoptosis and enhance chemotherapeutic cytotoxicity in head and neck squamous cell carcinoma. Oral Oncol 2011; 47: 8-15.
    • (2011) Oral Oncol , vol.47 , pp. 8-15
    • Roh, J.L.1    Kang, S.K.2
  • 74
    • 79551713220 scopus 로고    scopus 로고
    • Nutlin-3a is a potential therapeutic for ewing sarcoma
    • Pishas KI, Al-Ejeh F, Zinonos I, et al. Nutlin-3a is a potential therapeutic for ewing sarcoma. Clin Cancer Res 2011; 17: 494-504.
    • (2011) Clin Cancer Res , vol.17 , pp. 494-504
    • Pishas, K.I.1    Al-Ejeh, F.2    Zinonos, I.3
  • 75
    • 33749564973 scopus 로고    scopus 로고
    • MDM2 inhibition sensitizes neuroblastoma to chemotherapy-induced apoptotic cell death
    • Barbieri E, Mehta P, Chen Z, et al. MDM2 inhibition sensitizes neuroblastoma to chemotherapy-induced apoptotic cell death. Mol Cancer Ther 2006; 5: 2358-65.
    • (2006) Mol Cancer Ther , vol.5 , pp. 2358-2365
    • Barbieri, E.1    Mehta, P.2    Chen, Z.3
  • 76
    • 34249303144 scopus 로고    scopus 로고
    • Mouse double minute antagonist Nutlin-3a enhances chemotherapy-induced apoptosis in cancer cells with mutant p53 by activating E2F1
    • Ambrosini G, Sambol EB, Carvajal D, Vassilev LT, Singer S, Schwartz GK. Mouse double minute antagonist Nutlin-3a enhances chemotherapy-induced apoptosis in cancer cells with mutant p53 by activating E2F1. Oncogene 2007; 26: 3473-81.
    • (2007) Oncogene , vol.26 , pp. 3473-3481
    • Ambrosini, G.1    Sambol, E.B.2    Carvajal, D.3    Vassilev, L.T.4    Singer, S.5    Schwartz, G.K.6
  • 77
    • 67649442533 scopus 로고    scopus 로고
    • The MDM2 antagonist nutlin-3 sensitizes p53-null neuroblastoma cells to doxorubicin via E2F1 and TAp73
    • Peirce SK, Findley HW. The MDM2 antagonist nutlin-3 sensitizes p53-null neuroblastoma cells to doxorubicin via E2F1 and TAp73. Int J Oncol 2009; 34: 1395-402.
    • (2009) Int J Oncol , vol.34 , pp. 1395-1402
    • Peirce, S.K.1    Findley, H.W.2
  • 78
    • 77954646472 scopus 로고    scopus 로고
    • Disruption of p73-MDM2 binding synergizes with gemcitabine to induce apoptosis in HuCCT1 cholangiocarcinoma cell line with p53 mutation
    • Zheng T, Wang J, Chen X, et al. Disruption of p73-MDM2 binding synergizes with gemcitabine to induce apoptosis in HuCCT1 cholangiocarcinoma cell line with p53 mutation. Tumour Biol 2010; 31: 287-95.
    • (2010) Tumour Biol , vol.31 , pp. 287-295
    • Zheng, T.1    Wang, J.2    Chen, X.3
  • 79
    • 58349112761 scopus 로고    scopus 로고
    • Reversal of Pglycoprotein-mediated multidrug resistance by the murine double minute 2 antagonist nutlin-3
    • Michaelis M, Rothweiler F, Klassert D, et al. Reversal of Pglycoprotein-mediated multidrug resistance by the murine double minute 2 antagonist nutlin-3. Cancer Res 2009; 69: 416-21.
    • (2009) Cancer Res , vol.69 , pp. 416-421
    • Michaelis, M.1    Rothweiler, F.2    Klassert, D.3
  • 80
    • 0021956262 scopus 로고
    • Inhibition of tolbutamide metabolism by substituted imidazole drugs in vivo: Evidence for a structureactivity relationship
    • Back DJ, Tjia JF. Inhibition of tolbutamide metabolism by substituted imidazole drugs in vivo: evidence for a structureactivity relationship. Br J Pharmacol 1985; 85: 121-6.
    • (1985) Br J Pharmacol , vol.85 , pp. 121-126
    • Back, D.J.1    Tjia, J.F.2
  • 81
    • 33751291771 scopus 로고    scopus 로고
    • Nongenotoxic p53 activation protects cells against S-phase-specific chemotherapy
    • Kranz D, Dobbelstein M. Nongenotoxic p53 activation protects cells against S-phase-specific chemotherapy. Cancer Res 2006; 66: 10274-80.
    • (2006) Cancer Res , vol.66 , pp. 10274-10280
    • Kranz, D.1    Dobbelstein, M.2
  • 82
    • 34047271954 scopus 로고    scopus 로고
    • Nutlin-3 protects kidney cells during cisplatin therapy by suppressing Bax/Bak activation
    • Jiang M, Pabla N, Murphy RF, et al. Nutlin-3 protects kidney cells during cisplatin therapy by suppressing Bax/Bak activation. J Biol Chem 2007; 282: 2636-45.
    • (2007) J Biol Chem , vol.282 , pp. 2636-2645
    • Jiang, M.1    Pabla, N.2    Murphy, R.F.3
  • 83
    • 73149116617 scopus 로고    scopus 로고
    • Interactions of the Hdm2/p53 and proteasome pathways may enhance the antitumor activity of bortezomib
    • Ooi MG, Hayden PJ, Kotoula V, et al. Interactions of the Hdm2/p53 and proteasome pathways may enhance the antitumor activity of bortezomib. Clin Cancer Res 2009; 15: 7153-60.
    • (2009) Clin Cancer Res , vol.15 , pp. 7153-7160
    • Ooi, M.G.1    Hayden, P.J.2    Kotoula, V.3
  • 84
    • 78049305999 scopus 로고    scopus 로고
    • MDM2 antagonist Nutlin-3 enhances bortezomib-mediated mitochondrial apoptosis in TP53mutated mantle cell lymphoma
    • Jin L, Tabe Y, Kojima K, et al. MDM2 antagonist Nutlin-3 enhances bortezomib-mediated mitochondrial apoptosis in TP53mutated mantle cell lymphoma. Cancer Lett 2010; 299: 161-70.
    • (2010) Cancer Lett , vol.299 , pp. 161-170
    • Jin, L.1    Tabe, Y.2    Kojima, K.3
  • 85
    • 79952277220 scopus 로고    scopus 로고
    • MDM2 antagonist nutlin plus proteasome inhibitor velcade combination displays a synergistic anti-myeloma activity
    • Saha MN, Jiang H, Jayakar J, Reece D, Branch DR, Chang H. MDM2 antagonist nutlin plus proteasome inhibitor velcade combination displays a synergistic anti-myeloma activity. Cancer Biol Ther 2010; 9: 936-44.
    • (2010) Cancer Biol Ther , vol.9 , pp. 936-944
    • Saha, M.N.1    Jiang, H.2    Jayakar, J.3    Reece, D.4    Branch, D.R.5    Chang, H.6
  • 86
    • 79951831707 scopus 로고    scopus 로고
    • Dasatinib plus nutlin-3 shows synergistic antileukemic activity in both p53 wild-type and p53 mutated B chronic lymphocytic leukemias by inhibiting the Akt pathway
    • Zauli G, Voltan R, Bosco R, et al. Dasatinib plus nutlin-3 shows synergistic antileukemic activity in both p53 wild-type and p53 mutated B chronic lymphocytic leukemias by inhibiting the Akt pathway. Clin Cancer Res 2011; 17: 762-70.
    • (2011) Clin Cancer Res , vol.17 , pp. 762-770
    • Zauli, G.1    Voltan, R.2    Bosco, R.3
  • 87
    • 77951667031 scopus 로고    scopus 로고
    • Enhancement of imatinib-induced apoptosis of BCR/ABLexpressing cells by nutlin-3 through synergistic activation of the mitochondrial apoptotic pathway
    • Kurosu T, Wu N, Oshikawa G, Kagechika H, Miura O. Enhancement of imatinib-induced apoptosis of BCR/ABLexpressing cells by nutlin-3 through synergistic activation of the mitochondrial apoptotic pathway. Apoptosis 2010; 15: 608-20.
    • (2010) Apoptosis , vol.15 , pp. 608-620
    • Kurosu, T.1    Wu, N.2    Oshikawa, G.3    Kagechika, H.4    Miura, O.5
  • 88
    • 33644979375 scopus 로고    scopus 로고
    • Radiosensitization of lung cancer by nutlin, an inhibitor of murine double minute 2
    • Cao C, Shinohara ET, Subhawong TK, et al. Radiosensitization of lung cancer by nutlin, an inhibitor of murine double minute 2. Mol Cancer Ther 2006; 5: 411-7.
    • (2006) Mol Cancer Ther , vol.5 , pp. 411-417
    • Cao, C.1    Shinohara, E.T.2    Subhawong, T.K.3
  • 89
    • 33947324969 scopus 로고    scopus 로고
    • A dominant role for p53-dependent cellular senescence in radiosensitization of human prostate cancer cells
    • Lehmann BD, McCubrey JA, Jefferson HS, Paine MS, Chappell WH, Terrian DM. A dominant role for p53-dependent cellular senescence in radiosensitization of human prostate cancer cells. Cell Cycle 2007; 6: 595-605.
    • (2007) Cell Cycle , vol.6 , pp. 595-605
    • Lehmann, B.D.1    McCubrey, J.A.2    Jefferson, H.S.3    Paine, M.S.4    Chappell, W.H.5    Terrian, D.M.6
  • 90
    • 42549095546 scopus 로고    scopus 로고
    • Radiosensitization of prostate cancer by priming the wild-type p53-dependent cellular senescence pathway
    • Lehmann BD, McCubrey JA, Terrian DM. Radiosensitization of prostate cancer by priming the wild-type p53-dependent cellular senescence pathway. Cancer Biol Ther 2007; 6: 1165-70.
    • (2007) Cancer Biol Ther , vol.6 , pp. 1165-1170
    • Lehmann, B.D.1    McCubrey, J.A.2    Terrian, D.M.3
  • 91
    • 42249102761 scopus 로고    scopus 로고
    • Nutlin-3 radiosensitizes hypoxic prostate cancer cells independent of p53
    • Supiot S, Hill RP, Bristow RG. Nutlin-3 radiosensitizes hypoxic prostate cancer cells independent of p53. Mol Cancer Ther 2008; 7: 993-9.
    • (2008) Mol Cancer Ther , vol.7 , pp. 993-999
    • Supiot, S.1    Hill, R.P.2    Bristow, R.G.3
  • 92
    • 77954658151 scopus 로고    scopus 로고
    • Nutlin-3, the small-molecule inhibitor of MDM2, promotes senescence and radiosensitises laryngeal carcinoma cells harbouring wild-type p53
    • Arya AK, El-Fert A, Devling T, et al. Nutlin-3, the small-molecule inhibitor of MDM2, promotes senescence and radiosensitises laryngeal carcinoma cells harbouring wild-type p53. Br J Cancer 2010; 103: 186-95.
    • (2010) Br J Cancer , vol.103 , pp. 186-195
    • Arya, A.K.1    El-Fert, A.2    Devling, T.3
  • 93
    • 33645511223 scopus 로고    scopus 로고
    • Levels of HdmX expression dictate the sensitivity of normal and transformed cells to Nutlin-3
    • Patton JT, Mayo LD, Singhi AD, Gudkov AV, Stark GR, Jackson MW. Levels of HdmX expression dictate the sensitivity of normal and transformed cells to Nutlin-3. Cancer Res 2006; 66: 3169-76.
    • (2006) Cancer Res , vol.66 , pp. 3169-3176
    • Patton, J.T.1    Mayo, L.D.2    Singhi, A.D.3    Gudkov, A.V.4    Stark, G.R.5    Jackson, M.W.6
  • 94
    • 33845251005 scopus 로고    scopus 로고
    • Hdmx modulates the outcome of p53 activation in human tumor cells
    • Wade M, Wong ET, Tang M, Stommel JM, Wahl GM. Hdmx modulates the outcome of p53 activation in human tumor cells. J Biol Chem 2006; 281: 33036-44.
    • (2006) J Biol Chem , vol.281 , pp. 33036-33044
    • Wade, M.1    Wong, E.T.2    Tang, M.3    Stommel, J.M.4    Wahl, G.M.5
  • 95
    • 33845256980 scopus 로고    scopus 로고
    • MDMX overexpression prevents p53 activation by the MDM2 inhibitor Nutlin
    • Hu B, Gilkes DM, Farooqi B, Sebti SM, Chen J. MDMX overexpression prevents p53 activation by the MDM2 inhibitor Nutlin. J Biol Chem 2006; 281: 33030-5.
    • (2006) J Biol Chem , vol.281 , pp. 33030-33035
    • Hu, B.1    Gilkes, D.M.2    Farooqi, B.3    Sebti, S.M.4    Chen, J.5
  • 96
    • 45849116513 scopus 로고    scopus 로고
    • Elevated MDM2 boosts the apoptotic activity of p53-MDM2 binding inhibitors by facilitating MDMX degradation
    • Xia M, Knezevic D, Tovar C, Huang B, Heimbrook DC, Vassilev LT. Elevated MDM2 boosts the apoptotic activity of p53-MDM2 binding inhibitors by facilitating MDMX degradation. Cell Cycle 2008; 7: 1604-12.
    • (2008) Cell Cycle , vol.7 , pp. 1604-1612
    • Xia, M.1    Knezevic, D.2    Tovar, C.3    Huang, B.4    Heimbrook, D.C.5    Vassilev, L.T.6
  • 102
    • 76149111139 scopus 로고    scopus 로고
    • Patented inhibitors of p53-Mdm2 interaction (2006 2008)
    • Doemling A, University of Pittsburgh, USA Selective and dual-action p53/mdm2/mdm4 antagonists. WO 2008130614 2008 [103] Weber L
    • Doemling A, University of Pittsburgh, USA Selective and dual-action p53/mdm2/mdm4 antagonists. WO 2008130614 2008 [103] Weber L. Patented inhibitors of p53-Mdm2 interaction (2006 2008). Expert Opin Ther Pat 2010; 20: 179-91.
    • (2010) Expert Opin Ther Pat , vol.20 , pp. 179-191
  • 109
    • 33845335883 scopus 로고    scopus 로고
    • Antinociceptive and anti-inflammatory activities and QSAR studies on 2-substituted-4,5-diphenyl-1Himidazoles
    • Puratchikody A, Doble M. Antinociceptive and anti-inflammatory activities and QSAR studies on 2-substituted-4,5-diphenyl-1Himidazoles. Bioorg Med Chem 2007; 15: 1083-1090.
    • (2007) Bioorg Med Chem , vol.15 , pp. 1083-1090
    • Puratchikody, A.1    Doble, M.2
  • 110
    • 67651251300 scopus 로고    scopus 로고
    • QSAR studies on antiepileptic and locomotor in vivo activities of 4,5-diphenyl-1H-imidazoles
    • Puratchikody A, Doble M. QSAR studies on antiepileptic and locomotor in vivo activities of 4,5-diphenyl-1H-imidazoles. Chem Biol Drug Des 2009; 74: 173-182.
    • (2009) Chem Biol Drug Des , vol.74 , pp. 173-182
    • Puratchikody, A.1    Doble, M.2
  • 112
    • 77956042533 scopus 로고    scopus 로고
    • Highly enantioselective synthesis and cellular evaluation of spirooxindoles inspired by natural products
    • Antonchick AP, Gerding-Reimers C, Catarinella M, et al. Highly enantioselective synthesis and cellular evaluation of spirooxindoles inspired by natural products. Nat Chem 2010; 2: 735-40.
    • (2010) Nat Chem , vol.2 , pp. 735-740
    • Antonchick, A.P.1    Gerding-Reimers, C.2    Catarinella, M.3
  • 118
    • 79953672300 scopus 로고    scopus 로고
    • ChemInform Abstract: One-Pot Multicomponent Synthesis and Antimicrobial Evaluation of 2 (Indol-3-yl)-2-oxospiro(indoline-3,4 -pyran)Derivatives
    • doi: 10.1002/chin.201050138
    • Nandakumar A, Thirumurugan P, Perumal PT, Vembu P, Ponnuswamy MN, Ramesh P. ChemInform Abstract: One-Pot Multicomponent Synthesis and Antimicrobial Evaluation of 2 (Indol-3-yl)-2-oxospiro(indoline-3,4 -pyran)Derivatives. ChemInform 2010; 41: doi: 10.1002/chin.201050138.
    • (2010) ChemInform , vol.41
    • Nandakumar, A.1    Thirumurugan, P.2    Perumal, P.T.3    Vembu, P.4    Ponnuswamy, M.N.5    Ramesh, P.6
  • 121
    • 85036694403 scopus 로고    scopus 로고
    • Hoffman-La Roche Inc, USA Oxindole derivatives
    • US 7576082 B2
    • Luk K-CS, Sung-Sau; Zhang, Jing; Zhang, Zhuming, Hoffman-La Roche Inc, USA Oxindole derivatives. US 7576082 B2 2009.
    • (2009)
    • Luk, K.-C.S.1    Sung-Sau2    Zhang3    Jing4    Zhang5    Zhuming6
  • 122
    • 13944282529 scopus 로고    scopus 로고
    • Isoindolinone-based inhibitors of the MDM2-p53 protein-protein interaction
    • Hardcastle IR, Ahmed SU, Atkins H, et al. Isoindolinone-based inhibitors of the MDM2-p53 protein-protein interaction. Bioorg Med Chem Lett 2005; 15: 1515-20.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 1515-1520
    • Hardcastle, I.R.1    Ahmed, S.U.2    Atkins, H.3
  • 124
    • 22944473048 scopus 로고    scopus 로고
    • Structure-based design of potent non-peptide MDM2 inhibitors
    • Ding K, Lu Y, Nikolovska-Coleska Z, et al. Structure-based design of potent non-peptide MDM2 inhibitors. J Am Chem Soc 2005; 127: 10130-1.
    • (2005) J Am Chem Soc , vol.127 , pp. 10130-10131
    • Ding, K.1    Lu, Y.2    Nikolovska-Coleska, Z.3
  • 125
    • 33745154819 scopus 로고    scopus 로고
    • Structure-based design of spiro-oxindoles as potent, specific small-molecule inhibitors of the MDM2-p53 interaction
    • Ding K, Lu Y, Nikolovska-Coleska Z, et al. Structure-based design of spiro-oxindoles as potent, specific small-molecule inhibitors of the MDM2-p53 interaction. J Med Chem 2006; 49: 3432-5.
    • (2006) J Med Chem , vol.49 , pp. 3432-3435
    • Ding, K.1    Lu, Y.2    Nikolovska-Coleska, Z.3
  • 127
    • 56149109528 scopus 로고    scopus 로고
    • A small molecule that disrupts Mdm2-p53 binding activates p53, induces apoptosis and sensitizes lung cancer cells to chemotherapy
    • Sun SH, Zheng M, Ding K, Wang S, Sun Y. A small molecule that disrupts Mdm2-p53 binding activates p53, induces apoptosis and sensitizes lung cancer cells to chemotherapy. Cancer Biol Ther 2008; 7: 845-52.
    • (2008) Cancer Biol Ther , vol.7 , pp. 845-852
    • Sun, S.H.1    Zheng, M.2    Ding, K.3    Wang, S.4    Sun, Y.5
  • 128
    • 56149116043 scopus 로고    scopus 로고
    • Inhibition of MDM2-p53 feedback loop by various small molecules for potential cancer chemotherapy
    • Khan A, Lu H. Inhibition of MDM2-p53 feedback loop by various small molecules for potential cancer chemotherapy. Cancer Biol Ther 2008; 7: 853-5.
    • (2008) Cancer Biol Ther , vol.7 , pp. 853-855
    • Khan, A.1    Lu, H.2
  • 129
    • 41649102468 scopus 로고    scopus 로고
    • Temporal activation of p53 by a specific MDM2 inhibitor is selectively toxic to tumors and leads to complete tumor growth inhibition
    • Shangary S, Qin D, McEachern D, et al. Temporal activation of p53 by a specific MDM2 inhibitor is selectively toxic to tumors and leads to complete tumor growth inhibition. Proc Natl Acad Sci USA 2008; 105: 3933-8.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3933-3938
    • Shangary, S.1    Qin, D.2    McEachern, D.3
  • 130
    • 77958576777 scopus 로고    scopus 로고
    • Efficacy of MDM2 inhibitor MI-219 against lung cancer cells alone or in combination with MDM2 knockdown, a XIAP inhibitor or etoposide
    • Zheng M, Yang J, Xu X, Sebolt JT, Wang S, Sun Y. Efficacy of MDM2 inhibitor MI-219 against lung cancer cells alone or in combination with MDM2 knockdown, a XIAP inhibitor or etoposide. Anticancer Res 2010; 30: 3321-31.
    • (2010) Anticancer Res , vol.30 , pp. 3321-3331
    • Zheng, M.1    Yang, J.2    Xu, X.3    Sebolt, J.T.4    Wang, S.5    Sun, Y.6
  • 131
    • 77952800865 scopus 로고    scopus 로고
    • Reactivation of p53 by novel MDM2 inhibitors: Implications for pancreatic cancer therapy
    • Azmi AS, Philip PA, Aboukameel A, et al. Reactivation of p53 by novel MDM2 inhibitors: implications for pancreatic cancer therapy. Curr Cancer Drug Targets 2010; 10: 319-31.
    • (2010) Curr Cancer Drug Targets , vol.10 , pp. 319-331
    • Azmi, A.S.1    Philip, P.A.2    Aboukameel, A.3
  • 132
    • 73249140963 scopus 로고    scopus 로고
    • Potent and orally active smallmolecule inhibitors of the MDM2-p53 interaction
    • Yu S, Qin D, Shangary S, et al. Potent and orally active smallmolecule inhibitors of the MDM2-p53 interaction. J Med Chem 2009; 52: 7970-3.
    • (2009) J Med Chem , vol.52 , pp. 7970-7973
    • Yu, S.1    Qin, D.2    Shangary, S.3
  • 135
    • 85036702586 scopus 로고    scopus 로고
    • Hoffmann-La Roche Inc
    • US 7495007 B2
    • Chen LD, Qingjie; Liu, Jin-Jun; Yang, Song; Zhang, Zhuming, Hoffmann-La Roche Inc. USA Spiroindolinone derivatives US 7495007 B2 2009
    • (2009) USA Spiroindolinone Derivatives US
    • Chen, L.D.1
  • 141
    • 78649825828 scopus 로고    scopus 로고
    • Identification of the spiro(oxindole-3,3'-thiazolidine)-based derivatives as potential p53 activity modulators
    • Gomez-Monterrey I, Bertamino A, Porta A, et al. Identification of the spiro(oxindole-3,3'-thiazolidine)-based derivatives as potential p53 activity modulators. J Med Chem 2010; 53: 8319-29.
    • (2010) J Med Chem , vol.53 , pp. 8319-8329
    • Gomez-Monterrey, I.1    Bertamino, A.2    Porta, A.3
  • 143
    • 72549094296 scopus 로고    scopus 로고
    • An MDM2 antagonist (MI-319) restores p53 functions and increases the life span of orally treated follicular lymphoma bearing animals
    • Mohammad RM, Wu J, Azmi AS, et al. An MDM2 antagonist (MI-319) restores p53 functions and increases the life span of orally treated follicular lymphoma bearing animals. Mol Cancer 2009; 8: 115.
    • (2009) Mol Cancer , vol.8 , pp. 115
    • Mohammad, R.M.1    Wu, J.2    Azmi, A.S.3
  • 144
    • 77953492371 scopus 로고    scopus 로고
    • Structures of low molecular weight inhibitors bound to MDMX and MDM2 reveal new approaches for p53-MDMX/MDM2 antagonist drug discovery
    • Popowicz GM, Czarna A, Wolf S, et al. Structures of low molecular weight inhibitors bound to MDMX and MDM2 reveal new approaches for p53-MDMX/MDM2 antagonist drug discovery. Cell Cycle 2010; 9: 1104-11.
    • (2010) Cell Cycle , vol.9 , pp. 1104-1111
    • Popowicz, G.M.1    Czarna, A.2    Wolf, S.3
  • 145
    • 35948933091 scopus 로고    scopus 로고
    • Molecular basis for the inhibition of p53 by Mdmx
    • Popowicz GM, Czarna A, Rothweiler U, et al. Molecular basis for the inhibition of p53 by Mdmx. Cell Cycle 2007; 6: 2386-92.
    • (2007) Cell Cycle , vol.6 , pp. 2386-2392
    • Popowicz, G.M.1    Czarna, A.2    Rothweiler, U.3
  • 146
    • 48849117864 scopus 로고    scopus 로고
    • Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain
    • Popowicz GM, Czarna A, Holak TA. Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain. Cell Cycle 2008; 7: 2441-3.
    • (2008) Cell Cycle , vol.7 , pp. 2441-2443
    • Popowicz, G.M.1    Czarna, A.2    Holak, T.A.3
  • 147
    • 33749378169 scopus 로고    scopus 로고
    • Determinants of specificity of MDM2 for the activation domains of p53 and p65: Proline27 disrupts the MDM2-binding motif of p53
    • Zondlo SC, Lee AE, Zondlo NJ. Determinants of specificity of MDM2 for the activation domains of p53 and p65: proline27 disrupts the MDM2-binding motif of p53. Biochemistry 2006; 45: 11945-57.
    • (2006) Biochemistry , vol.45 , pp. 11945-11957
    • Zondlo, S.C.1    Lee, A.E.2    Zondlo, N.J.3
  • 148
    • 34548780897 scopus 로고    scopus 로고
    • Efficient p53 activation and apoptosis by simultaneous disruption of binding to MDM2 and MDMX
    • Hu B, Gilkes DM, Chen J. Efficient p53 activation and apoptosis by simultaneous disruption of binding to MDM2 and MDMX. Cancer Res 2007; 67: 8810-7.
    • (2007) Cancer Res , vol.67 , pp. 8810-8817
    • Hu, B.1    Gilkes, D.M.2    Chen, J.3
  • 149
    • 66149092109 scopus 로고    scopus 로고
    • Crystal Structures of Human MdmX (HdmX) in Complex with p53 Peptide Analogues Reveal Surprising Conformational Changes
    • Kallen J, Goepfert A, Blechschmidt A, et al. Crystal Structures of Human MdmX (HdmX) in Complex with p53 Peptide Analogues Reveal Surprising Conformational Changes. J Biol Chem 2009; 284: 8812-21.
    • (2009) J Biol Chem , vol.284 , pp. 8812-8821
    • Kallen, J.1    Goepfert, A.2    Blechschmidt, A.3
  • 150
    • 63849271797 scopus 로고    scopus 로고
    • Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX
    • Pazgier M, Liu M, Zou G, et al. Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX. Proc Natl Acad Sci USA 2009; 106: 4665-70.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4665-4670
    • Pazgier, M.1    Liu, M.2    Zou, G.3
  • 152
    • 65949087007 scopus 로고    scopus 로고
    • High affinity interaction of the p53 peptide-analogue with human Mdm2 and Mdmx
    • Czarna A, Popowicz GM, Pecak A, Wolf S, Dubin G, Holak TA. High affinity interaction of the p53 peptide-analogue with human Mdm2 and Mdmx. Cell Cycle 2009; 8: 1176-84.
    • (2009) Cell Cycle , vol.8 , pp. 1176-1184
    • Czarna, A.1    Popowicz, G.M.2    Pecak, A.3    Wolf, S.4    Dubin, G.5    Holak, T.A.6
  • 153
    • 0035895350 scopus 로고    scopus 로고
    • Chalcone derivatives antagonize interactions between the human oncoprotein MDM2 and p53
    • Stoll R, Renner C, Hansen S, et al. Chalcone derivatives antagonize interactions between the human oncoprotein MDM2 and p53. Biochemistry 2001; 40: 336-44.
    • (2001) Biochemistry , vol.40 , pp. 336-344
    • Stoll, R.1    Renner, C.2    Hansen, S.3
  • 156
    • 33745276531 scopus 로고    scopus 로고
    • A boronic-chalcone derivative exhibits potent anticancer activity through inhibition of the proteasome
    • Achanta G, Modzelewska A, Feng L, Khan SR, Huang P. A boronic-chalcone derivative exhibits potent anticancer activity through inhibition of the proteasome. Mol Pharmacol 2006; 70: 426-33.
    • (2006) Mol Pharmacol , vol.70 , pp. 426-433
    • Achanta, G.1    Modzelewska, A.2    Feng, L.3    Khan, S.R.4    Huang, P.5
  • 157
    • 11144315535 scopus 로고    scopus 로고
    • Small molecule RITA binds to p53, blocks p53-HDM-2 interaction and activates p53 function in tumors
    • Issaeva N, Bozko P, Enge M, et al. Small molecule RITA binds to p53, blocks p53-HDM-2 interaction and activates p53 function in tumors. Nat Med 2004; 10: 1321-8.
    • (2004) Nat Med , vol.10 , pp. 1321-1328
    • Issaeva, N.1    Bozko, P.2    Enge, M.3
  • 158
    • 77953562379 scopus 로고    scopus 로고
    • Rescue of the apoptotic-inducing function of mutant p53 by small molecule RITA
    • Zhao CY, Grinkevich VV, Nikulenkov F, Bao W, Selivanova G. Rescue of the apoptotic-inducing function of mutant p53 by small molecule RITA. Cell Cycle 2010; 9: 1847-55.
    • (2010) Cell Cycle , vol.9 , pp. 1847-1855
    • Zhao, C.Y.1    Grinkevich, V.V.2    Nikulenkov, F.3    Bao, W.4    Selivanova, G.5
  • 159
    • 30744449974 scopus 로고    scopus 로고
    • NMR indicates that the small molecule RITA does not block p53MDM2 binding in vitro
    • author reply 1136-7
    • Krajewski M, Ozdowy P, D'Silva L, Rothweiler U, Holak TA. NMR indicates that the small molecule RITA does not block p53MDM2 binding in vitro. Nat Med 2005; 11: 1135-6; author reply 1136-7.
    • (2005) Nat Med , vol.11 , pp. 1135-1136
    • Krajewski, M.1    Ozdowy, P.2    D'Silva, L.3    Rothweiler, U.4    Holak, T.A.5
  • 160
    • 67649646649 scopus 로고    scopus 로고
    • Identification of a disruptor of the MDM2-p53 protein-protein interaction facilitated by highthroughput in silico docking
    • Lawrence HR, Li Z, Yip ML, et al. Identification of a disruptor of the MDM2-p53 protein-protein interaction facilitated by highthroughput in silico docking. Bioorg Med Chem Lett 2009; 19: 3756-9.
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 3756-3759
    • Lawrence, H.R.1    Li, Z.2    Yip, M.L.3
  • 163
    • 67649369143 scopus 로고    scopus 로고
    • JNJ-26854165 a novel HDM2 antagonist in clinical development showing broad-spectrum preclinical antitumour activity against solid malignancies
    • Arts J PM, Valckx A, et al. JNJ-26854165 a novel HDM2 antagonist in clinical development showing broad-spectrum preclinical antitumour activity against solid malignancies. Proc Am Assoc Cancer Res AACR; 2008
    • (2008) Proc Am Assoc Cancer Res AACR
    • Arts, J.P.M.1    Valckx, A.2
  • 164
    • 67649316859 scopus 로고    scopus 로고
    • Identification of a novel orally active HDM2 antagonist with potent antitumour activity
    • Schoentjes B LJ, Meyer C. Identification of a novel orally active HDM2 antagonist with potent antitumour activity. Natl Med Chem Symp 2008
    • (2008) Natl Med Chem Symp
    • Schoentjes, B.L.J.1    Meyer, C.2
  • 167
    • 33745645832 scopus 로고    scopus 로고
    • Discovery of a nanomolar inhibitor of the human murine double minute 2 (MDM2)-p53 interaction through an integrated, virtual database screening strategy
    • Lu Y, Nikolovska-Coleska Z, Fang X, et al. Discovery of a nanomolar inhibitor of the human murine double minute 2 (MDM2)-p53 interaction through an integrated, virtual database screening strategy. J Med Chem 2006; 49: 3759-62.
    • (2006) J Med Chem , vol.49 , pp. 3759-3762
    • Lu, Y.1    Nikolovska-Coleska, Z.2    Fang, X.3
  • 168
    • 79951717280 scopus 로고    scopus 로고
    • Clioquinol a novel copper-dependent and independent proteasome inhibitor
    • Schimmer AD. Clioquinol a novel copper-dependent and independent proteasome inhibitor. Curr Cancer Drug Targets 2011.
    • (2011) Curr Cancer Drug Targets
    • Schimmer, A.D.1
  • 169
    • 54949124884 scopus 로고    scopus 로고
    • The toxicology of Clioquinol
    • Mao X, Schimmer AD. The toxicology of Clioquinol. Toxicol Lett 2008; 182: 1-6.
    • (2008) Toxicol Lett , vol.182 , pp. 1-6
    • Mao, X.1    Schimmer, A.D.2
  • 172
    • 77954311112 scopus 로고    scopus 로고
    • Design and Synthesis of Functionalized Trisaccharides as p53-Peptide Mimics
    • Sakurai K, Kahne D. Design and Synthesis of Functionalized Trisaccharides as p53-Peptide Mimics. Tetrahedron Lett 2010; 51: 3724-3727.
    • (2010) Tetrahedron Lett , vol.51 , pp. 3724-3727
    • Sakurai, K.1    Kahne, D.2
  • 173
    • 77954850783 scopus 로고    scopus 로고
    • Robust generation of lead compounds for protein-protein interactions by computational and MCR chemistry: P53/Hdm2 antagonists
    • Czarna A, Beck B, Srivastava S, et al. Robust generation of lead compounds for protein-protein interactions by computational and MCR chemistry: p53/Hdm2 antagonists. Angew Chem Int Ed Engl 2010; 49: 5352-6.
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 5352-5356
    • Czarna, A.1    Beck, B.2    Srivastava, S.3
  • 174
    • 18744406282 scopus 로고    scopus 로고
    • Differentiation of Hdm2-mediated p53 ubiquitination and Hdm2 autoubiquitination activity by small molecular weight inhibitors
    • Lai Z, Yang T, Kim YB, et al. Differentiation of Hdm2-mediated p53 ubiquitination and Hdm2 autoubiquitination activity by small molecular weight inhibitors. Proc Natl Acad Sci USA 2002; 99: 14734-9.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14734-14739
    • Lai, Z.1    Yang, T.2    Kim, Y.B.3
  • 175
    • 20144389192 scopus 로고    scopus 로고
    • Assay for ubiquitin ligase activity: High-throughput screen for inhibitors of HDM2
    • Davydov IV, Woods D, Safiran YJ, et al. Assay for ubiquitin ligase activity: high-throughput screen for inhibitors of HDM2. J Biomol Screen 2004; 9: 695-703.
    • (2004) J Biomol Screen , vol.9 , pp. 695-703
    • Davydov, I.V.1    Woods, D.2    Safiran, Y.J.3
  • 176
    • 36549047979 scopus 로고    scopus 로고
    • A high-throughput screen measuring ubiquitination of p53 by human mdm2
    • Murray MF, Jurewicz AJ, Martin JD, et al. A high-throughput screen measuring ubiquitination of p53 by human mdm2. J Biomol Screen 2007; 12: 1050-8.
    • (2007) J Biomol Screen , vol.12 , pp. 1050-1058
    • Murray, M.F.1    Jurewicz, A.J.2    Martin, J.D.3
  • 177
    • 20444369867 scopus 로고    scopus 로고
    • Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells
    • Yang Y, Ludwig RL, Jensen JP, et al. Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells. Cancer Cell 2005; 7: 547-59.
    • (2005) Cancer Cell , vol.7 , pp. 547-559
    • Yang, Y.1    Ludwig, R.L.2    Jensen, J.P.3
  • 178
    • 53349153446 scopus 로고    scopus 로고
    • Targeting tumor cells expressing p53 with a water-soluble inhibitor of Hdm2
    • Kitagaki J, Agama KK, Pommier Y, Yang Y, Weissman AM. Targeting tumor cells expressing p53 with a water-soluble inhibitor of Hdm2. Mol Cancer Ther 2008; 7: 2445-54.
    • (2008) Mol Cancer Ther , vol.7 , pp. 2445-2454
    • Kitagaki, J.1    Agama, K.K.2    Pommier, Y.3    Yang, Y.4    Weissman, A.M.5
  • 179
    • 70949084205 scopus 로고    scopus 로고
    • Discovery and optimization of chromenotriazolopyrimidines as potent inhibitors of the mouse double minute 2-tumor protein 53 protein-protein interaction
    • Allen JG, Bourbeau MP, Wohlhieter GE, et al. Discovery and optimization of chromenotriazolopyrimidines as potent inhibitors of the mouse double minute 2-tumor protein 53 protein-protein interaction. J Med Chem 2009; 52: 7044-53.
    • (2009) J Med Chem , vol.52 , pp. 7044-7053
    • Allen, J.G.1    Bourbeau, M.P.2    Wohlhieter, G.E.3
  • 180
    • 77951224332 scopus 로고    scopus 로고
    • Identification and characterization of the first small molecule inhibitor of MDMX
    • Reed D, Shen Y, Shelat AA, et al. Identification and characterization of the first small molecule inhibitor of MDMX. J Biol Chem 2010; 285: 10786-96.
    • (2010) J Biol Chem , vol.285 , pp. 10786-10796
    • Reed, D.1    Shen, Y.2    Shelat, A.A.3
  • 182
    • 77956563054 scopus 로고    scopus 로고
    • The novel tryptamine derivative JNJ-26854165 induces wild-type p53and E2F1-mediated apoptosis in acute myeloid and lymphoid leukemias
    • Kojima K, Burks JK, Arts J, Andreeff M. The novel tryptamine derivative JNJ-26854165 induces wild-type p53and E2F1-mediated apoptosis in acute myeloid and lymphoid leukemias. Mol Cancer Ther 2010; 9: 2545-57.
    • (2010) Mol Cancer Ther , vol.9 , pp. 2545-2557
    • Kojima, K.1    Burks, J.K.2    Arts, J.3    Andreeff, M.4
  • 184
    • 79953652907 scopus 로고    scopus 로고
    • Inhibition of the human double minute(HDM)-2 E3 ubiquitin ligase activates different programmed cell death (PCD) pathways in models of Non-Hodgkin lymphoma (NHL) with wild type (wt) and mutant (mut) p53
    • Jones RJ, Arts J, Orlowski RZ. Inhibition of the human double minute(HDM)-2 E3 ubiquitin ligase activates different programmed cell death (PCD) pathways in models of Non-Hodgkin lymphoma (NHL) with wild type (wt) and mutant (mut) p53. 50th ASH Annual Meeting and Exposition; San Francisco; 2008
    • (2008) 50th ASH Annual Meeting and Exposition; San Francisco
    • Jones, R.J.1    Arts, J.2    Orlowski, R.Z.3
  • 185
    • 84873413419 scopus 로고    scopus 로고
    • Preclinical and clinical pharmacodynamic activity of JNJ-26854165: A novel HDM2 antagonist in clinical development
    • Arts J, Smans K, Andries L, et al. Preclinical and clinical pharmacodynamic activity of JNJ-26854165: a novel HDM2 antagonist in clinical development. 100th AACR Annual Meeting; Denver; 2009
    • (2009) 100th AACR Annual Meeting; Denver
    • Arts, J.1    Smans, K.2    Andries, L.3
  • 190
    • 84867458226 scopus 로고    scopus 로고
    • Small molecule agents targeting the p53-MDM2 pathway for cancer therapy
    • DOI: 10.1002/ med.20236
    • Wang W, Hu Y. Small molecule agents targeting the p53-MDM2 pathway for cancer therapy. Med Res Rev 2011; DOI: 10.1002/ med.20236.
    • (2011) Med Res Rev
    • Wang, W.1    Hu, Y.2
  • 191
    • 85036721868 scopus 로고    scopus 로고
    • Clinical trials.gov USNIH, A multi-center, open-label, phase I study of single agent R7112 administered orally in patients with advanced malignancies, except all forms of leukaemia
    • Clinical trials.gov USNIH. A multi-center, open-label, phase I study of single agent R7112 administered orally in patients with advanced malignancies, except all forms of leukaemia. http://clinicaltrials.gov/ct2/show/record/NCT00559533?term=RO5045337&rank=4
  • 192
    • 85036690993 scopus 로고    scopus 로고
    • Clinical trials.gov USNIH, An open label study to investigate the maximum tolerated dose of R7112 in patients with acute myelogenous leukemia (AML), acute lymphocytic leukemia (ALL), chronic myelogenous leukemia (CML) in blast phase, or refractory chronic lymphocytic leukemia/small cell lymphocytic lymphoma(CLL/SCLL)
    • Clinical trials.gov USNIH. An open label study to investigate the maximum tolerated dose of R7112 in patients with acute myelogenous leukemia (AML), acute lymphocytic leukemia (ALL), chronic myelogenous leukemia (CML) in blast phase, or refractory chronic lymphocytic leukemia/small cell lymphocytic lymphoma(CLL/SCLL). http://clinicaltrials.gov/ct2/show? term=RO5045337&rank=3
  • 193
    • 79953653639 scopus 로고    scopus 로고
    • A multi-center, open-label, phase I study of single agent RG7112, a first in class p53-MDM2 antagonist, in patients with relapsed/refractory acute myeloid and lymphoid leukemias (AML/ALL) and refractory chronic lymphocytic leukemia/small cell lymphocytic lymphomas (CLL/SCLL)
    • Andreeff M, Kojima K, Padmanabhan S, et al. A multi-center, open-label, phase I study of single agent RG7112, a first in class p53-MDM2 antagonist, in patients with relapsed/refractory acute myeloid and lymphoid leukemias (AML/ALL) and refractory chronic lymphocytic leukemia/small cell lymphocytic lymphomas (CLL/SCLL). 52nd ASH Annual Meeting and Exposition; Orlando; 2010
    • (2010) 52nd ASH Annual Meeting and Exposition; Orlando
    • Andreeff, M.1    Kojima, K.2    Padmanabhan, S.3
  • 194
    • 85036694074 scopus 로고    scopus 로고
    • Clinical trials.gov USNIH, An exploratory biomarker study of RO5045337 in patients with liposarcomas prior to debulking surgery
    • Clinical trials.gov USNIH. An exploratory biomarker study of RO5045337 in patients with liposarcomas prior to debulking surgery. http://clinicaltrials.gov/ct2/show?term=RO5045337&rank=2
  • 195
    • 85036708592 scopus 로고    scopus 로고
    • Clinical trials.gov USNIH, An open-label, randomized 3-way crossover, study to examine the food-effect on pharmacokinetics of the current formulation and relative bioavailability of two new formulations for RO5045337 in patients with solid tumors includinglymphoma
    • Clinical trials.gov USNIH. An open-label, randomized 3-way crossover, study to examine the food-effect on pharmacokinetics of the current formulation and relative bioavailability of two new formulations for RO5045337 in patients with solid tumors includinglymphoma. http://clinicaltrials.gov/ct2/show?term=RO5045337&rank=1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.